{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,24]],"date-time":"2026-09-24T01:37:42Z","timestamp":1790213862662,"version":"4.1.0"},"reference-count":606,"publisher":"MDPI AG","issue":"4","license":[{"start":{"date-parts":[[2020,3,30]],"date-time":"2020-03-30T00:00:00Z","timestamp":1585526400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Cells"],"abstract":"<jats:p>Autophagy is a catabolic process involving vacuolar sequestration of intracellular components and their targeting to lysosomes for degradation, thus supporting nutrient recycling and energy regeneration. Accumulating evidence indicates that in addition to being a bulk, nonselective degradation mechanism, autophagy may selectively eliminate damaged mitochondria to promote mitochondrial turnover, a process termed \u201cmitophagy\u201d. Mitophagy sequesters dysfunctional mitochondria via ubiquitination and cargo receptor recognition and has emerged as an important event in the regulation of liver physiology. Recent studies have shown that mitophagy may participate in the pathogenesis of various liver diseases, such as liver injury, liver steatosis\/fatty liver disease, hepatocellular carcinoma, viral hepatitis, and hepatic fibrosis. This review summarizes the current knowledge on the molecular regulations and functions of mitophagy in liver physiology and the roles of mitophagy in the development of liver-related diseases. Furthermore, the therapeutic implications of targeting hepatic mitophagy to design a new strategy to cure liver diseases are discussed.<\/jats:p>","DOI":"10.3390\/cells9040831","type":"journal-article","created":{"date-parts":[[2020,4,1]],"date-time":"2020-04-01T05:52:30Z","timestamp":1585720350000},"page":"831","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":84,"title":["Mitophagy in the Pathogenesis of Liver Diseases"],"prefix":"10.3390","volume":"9","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-0471-0806","authenticated-orcid":false,"given":"Po-Yuan","family":"Ke","sequence":"first","affiliation":[{"name":"Department of Biochemistry &amp; Molecular Biology and Graduate Institute of Biomedical Sciences, College of Medicine, Chang Gung University, Taoyuan 33302, Taiwan"},{"name":"Liver Research Center, Chang Gung Memorial Hospital, Taoyuan 33305, Taiwan"},{"name":"Division of Allergy, Immunology, and Rheumatology, Chang Gung Memorial Hospital, Taoyuan 33305, Taiwan"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2020,3,30]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"14","DOI":"10.1172\/JCI73938","article-title":"Development of autophagy inducers in clinical medicine","volume":"125","author":"Levine","year":"2015","journal-title":"J. Clin. Investig."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"651","DOI":"10.1056\/NEJMra1205406","article-title":"Autophagy in human health and disease","volume":"368","author":"Choi","year":"2013","journal-title":"N. Engl. J. Med."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"233","DOI":"10.1038\/s41556-018-0037-z","article-title":"Cargo recognition and degradation by selective autophagy","volume":"20","author":"Gatica","year":"2018","journal-title":"Nat. Cell Biol."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"1714","DOI":"10.1016\/j.jmb.2016.02.004","article-title":"Mechanisms of Selective Autophagy","volume":"428","author":"Zaffagnini","year":"2016","journal-title":"J. Mol. Biol."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"10","DOI":"10.1016\/j.devcel.2017.02.016","article-title":"Cleaning House: Selective Autophagy of Organelles","volume":"41","author":"Anding","year":"2017","journal-title":"Dev. Cell"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"R170","DOI":"10.1016\/j.cub.2018.01.004","article-title":"Mitophagy and Quality Control Mechanisms in Mitochondrial Maintenance","volume":"28","author":"Pickles","year":"2018","journal-title":"Curr. Biol."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"206","DOI":"10.1016\/j.jmb.2019.06.032","article-title":"Outstanding Questions in Mitophagy: What We Do and Do Not Know","volume":"432","author":"Ganley","year":"2020","journal-title":"J. Mol. Biol."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"1812","DOI":"10.1161\/CIRCRESAHA.117.311082","article-title":"Autophagy and Mitophagy in Cardiovascular Disease","volume":"120","author":"Kroemer","year":"2017","journal-title":"Circ. Res."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"66","DOI":"10.1016\/j.neulet.2018.04.004","article-title":"Multiple pathways for mitophagy: A neurodegenerative conundrum for Parkinson\u2019s disease","volume":"697","author":"Chu","year":"2019","journal-title":"Neurosci. Lett."},{"key":"ref_10","doi-asserted-by":"crossref","unstructured":"Liu, L., Liao, X., Wu, H., Li, Y., Zhu, Y., and Chen, Q. (2020). Mitophagy and its contribution to metabolic and aging associated disorders. Antioxid. Redox Signal.","DOI":"10.1089\/ars.2019.8013"},{"key":"ref_11","doi-asserted-by":"crossref","unstructured":"Wang, Y., Cai, J., Tang, C., and Dong, Z. (2020). Mitophagy in Acute Kidney Injury and Kidney Repair. Cells, 9.","DOI":"10.3390\/cells9020338"},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1016\/j.jhep.2019.08.026","article-title":"Autophagy in hepatic adaptation to stress","volume":"72","author":"Hazari","year":"2020","journal-title":"J. Hepatol."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"349","DOI":"10.1083\/jcb.3.3.349","article-title":"Cellular differentiation in the kidneys of newborn mice studies with the electron microscope","volume":"3","author":"Clark","year":"1957","journal-title":"J. Biophys. Biochem. Cytol."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"198","DOI":"10.1083\/jcb.12.1.198","article-title":"Cytoplasmic components in hepatic cell lysosomes","volume":"12","author":"Ashford","year":"1962","journal-title":"J. Cell Biol."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"140","DOI":"10.1083\/jcb.15.1.140","article-title":"Cytolysomes and mitochondrial degeneration","volume":"15","author":"Novikoff","year":"1962","journal-title":"J. Cell Biol."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"136","DOI":"10.1083\/jcb.6.1.136","article-title":"The proximal tubule cell in experimental hydronephrosis","volume":"6","author":"Novikoff","year":"1959","journal-title":"J. Biophys. Biochem. Cytol."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"435","DOI":"10.1146\/annurev.ph.28.030166.002251","article-title":"Functions of lysosomes","volume":"28","author":"Wattiaux","year":"1966","journal-title":"Annu. Rev. Physiol."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"740","DOI":"10.4161\/auto.6398","article-title":"Autophagy revisited: A conversation with Christian de Duve","volume":"4","author":"Klionsky","year":"2008","journal-title":"Autophagy"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"437","DOI":"10.1083\/jcb.33.2.437","article-title":"Influence of glucagon, an inducer of cellular autophagy, on some physical properties of rat liver lysosomes","volume":"33","author":"Deter","year":"1967","journal-title":"J. Cell Biol."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"C11","DOI":"10.1083\/jcb.35.2.C11","article-title":"Participation of lysosomes in cellular autophagy induced in rat liver by glucagon","volume":"35","author":"Deter","year":"1967","journal-title":"J. Cell Biol."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"174","DOI":"10.1038\/270174a0","article-title":"Induction of autophagy by amino-acid deprivation in perfused rat liver","volume":"270","author":"Mortimore","year":"1977","journal-title":"Nature"},{"key":"ref_22","first-page":"1691","article-title":"Inhibition by insulin of the physiological autophagic breakdown of cell organelles","volume":"36","author":"Pfeifer","year":"1977","journal-title":"Acta Biol. Med. Ger."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"152","DOI":"10.1083\/jcb.78.1.152","article-title":"Inhibition by insulin of the formation of autophagic vacuoles in rat liver. A morphometric approach to the kinetics of intracellular degradation by autophagy","volume":"78","author":"Pfeifer","year":"1978","journal-title":"J. Cell Biol."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"194","DOI":"10.1016\/0014-5793(81)80600-X","article-title":"Inhibition of autophagic sequestration and endogenous protein degradation in isolated rat hepatocytes by methylated adenosine derivatives","volume":"134","author":"Kovacs","year":"1981","journal-title":"FEBS Lett."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"522","DOI":"10.1006\/excr.1995.1187","article-title":"Disruption of the cytokeratin cytoskeleton and inhibition of hepatocytic autophagy by okadaic acid","volume":"218","author":"Blankson","year":"1995","journal-title":"Exp. Cell Res."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"633","DOI":"10.1042\/bj2840633","article-title":"Protein kinase-dependent effects of okadaic acid on hepatocytic autophagy and cytoskeletal integrity","volume":"284","author":"Holen","year":"1992","journal-title":"Biochem. J."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"12823","DOI":"10.1074\/jbc.270.21.12823","article-title":"Inhibition of autophagy and multiple steps in asialoglycoprotein endocytosis by inhibitors of tyrosine protein kinases (tyrphostins)","volume":"270","author":"Holen","year":"1995","journal-title":"J. Biol. Chem."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"1889","DOI":"10.1073\/pnas.79.6.1889","article-title":"3-Methyladenine: Specific inhibitor of autophagic\/lysosomal protein degradation in isolated rat hepatocytes","volume":"79","author":"Seglen","year":"1982","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1016\/0304-4165(81)90189-6","article-title":"Inhibition of hepatocytic protein degradation by methylaminopurines and inhibitors of protein synthesis","volume":"676","author":"Kovacs","year":"1981","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"128","DOI":"10.1016\/0167-4889(87)90167-4","article-title":"Temperature dependence of protein degradation, autophagic sequestration and mitochondrial sugar uptake in rat hepatocytes","volume":"929","author":"Gordon","year":"1987","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1111\/j.1432-1033.1987.tb11011.x","article-title":"Energy dependence of autophagic protein degradation in isolated rat hepatocytes","volume":"164","author":"Plomp","year":"1987","journal-title":"Eur. J. Biochem."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"40","DOI":"10.1016\/0006-291X(88)90556-6","article-title":"Prelysosomal convergence of autophagic and endocytic pathways","volume":"151","author":"Gordon","year":"1988","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"573","DOI":"10.1177\/38.4.2319125","article-title":"Characterization of the isolation membranes and the limiting membranes of autophagosomes in rat hepatocytes by lectin cytochemistry","volume":"38","author":"Yamamoto","year":"1990","journal-title":"J. Histochem. Cytochem."},{"key":"ref_34","first-page":"67","article-title":"Formation of autophagosomes during degradation of excess peroxisomes induced by administration of dioctyl phthalate","volume":"61","author":"Yokota","year":"1993","journal-title":"Eur. J. Cell Biol."},{"key":"ref_35","first-page":"372","article-title":"Formation of autophagosomes during degradation of excess peroxisomes induced by di-(2-ethylhexyl)phthalate treatment. II. Immunocytochemical analysis of early and late autophagosomes","volume":"62","author":"Yokota","year":"1993","journal-title":"Eur. J. Cell Biol."},{"key":"ref_36","first-page":"15","article-title":"Formation of autophagosomes during degradation of excess peroxisomes induced by di-(2-ethylhexyl)-phthalate treatment. III. Fusion of early autophagosomes with lysosomal compartments","volume":"66","author":"Yokota","year":"1995","journal-title":"Eur. J. Cell Biol."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1083\/jcb.136.1.61","article-title":"The autophagic and endocytic pathways converge at the nascent autophagic vacuoles","volume":"136","author":"Liou","year":"1997","journal-title":"J. Cell Biol."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"504","DOI":"10.1006\/excr.1995.1402","article-title":"Ultrastructural and immunocytochemical characterization of autophagic vacuoles in isolated hepatocytes: Effects of vinblastine and asparagine on vacuole distributions","volume":"221","author":"Fengsrud","year":"1995","journal-title":"Exp. Cell Res."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1016\/0014-4827(90)90245-6","article-title":"Immunocytochemical study of the surrounding envelope of autophagic vacuoles in cultured rat hepatocytes","volume":"189","author":"Furuno","year":"1990","journal-title":"Exp. Cell Res."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"301","DOI":"10.1083\/jcb.119.2.301","article-title":"Autophagy in yeast demonstrated with proteinase-deficient mutants and conditions for its induction","volume":"119","author":"Takeshige","year":"1992","journal-title":"J. Cell Biol."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1016\/0014-5793(93)80398-E","article-title":"Isolation and characterization of autophagy-defective mutants of Saccharomyces cerevisiae","volume":"333","author":"Tsukada","year":"1993","journal-title":"FEBS Lett."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"126","DOI":"10.1006\/bbrc.1995.1636","article-title":"Novel system for monitoring autophagy in the yeast Saccharomyces cerevisiae","volume":"210","author":"Noda","year":"1995","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"17621","DOI":"10.1074\/jbc.271.30.17621","article-title":"Genetic and phenotypic overlap between autophagy and the cytoplasm to vacuole protein targeting pathway","volume":"271","author":"Harding","year":"1996","journal-title":"J. Biol. Chem."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"1068","DOI":"10.1128\/jb.179.4.1068-1076.1997","article-title":"AUT1, a gene essential for autophagocytosis in the yeast Saccharomyces cerevisiae","volume":"179","author":"Schlumpberger","year":"1997","journal-title":"J. Bacteriol."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"3875","DOI":"10.1128\/jb.179.12.3875-3883.1997","article-title":"AUT3, a serine\/threonine kinase gene, is essential for autophagocytosis in Saccharomyces cerevisiae","volume":"179","author":"Straub","year":"1997","journal-title":"J. Bacteriol."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"3597","DOI":"10.1093\/emboj\/17.13.3597","article-title":"Aut2p and Aut7p, two novel microtubule-associated proteins are essential for delivery of autophagic vesicles to the vacuole","volume":"17","author":"Lang","year":"1998","journal-title":"EMBO J."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"539","DOI":"10.1016\/S1534-5807(03)00296-X","article-title":"A unified nomenclature for yeast autophagy-related genes","volume":"5","author":"Klionsky","year":"2003","journal-title":"Dev. Cell"},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"438","DOI":"10.4161\/auto.6.4.12244","article-title":"A comprehensive glossary of autophagy-related molecules and processes","volume":"6","author":"Klionsky","year":"2010","journal-title":"Autophagy"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"1273","DOI":"10.4161\/auto.7.11.17661","article-title":"A comprehensive glossary of autophagy-related molecules and processes (2nd edition)","volume":"7","author":"Klionsky","year":"2011","journal-title":"Autophagy"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"521","DOI":"10.1038\/s41556-018-0092-5","article-title":"A brief history of autophagy from cell biology to physiology and disease","volume":"20","author":"Mizushima","year":"2018","journal-title":"Nat. Cell Biol."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"1811","DOI":"10.15252\/embj.201796697","article-title":"Molecular definitions of autophagy and related processes","volume":"36","author":"Galluzzi","year":"2017","journal-title":"EMBO J."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"24","DOI":"10.1038\/cr.2013.168","article-title":"The machinery of macroautophagy","volume":"24","author":"Feng","year":"2014","journal-title":"Cell Res."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"323","DOI":"10.1038\/nature09782","article-title":"Autophagy in immunity and inflammation","volume":"469","author":"Levine","year":"2011","journal-title":"Nature"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"1069","DOI":"10.1038\/nature06639","article-title":"Autophagy fights disease through cellular self-digestion","volume":"451","author":"Mizushima","year":"2008","journal-title":"Nature"},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1172\/JCI73946","article-title":"Essential role for autophagy in life span extension","volume":"125","author":"Madeo","year":"2015","journal-title":"J. Clin. Investig."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"1015","DOI":"10.1016\/j.neuron.2017.01.022","article-title":"Autophagy and Neurodegeneration: Pathogenic Mechanisms and Therapeutic Opportunities","volume":"93","author":"Menzies","year":"2017","journal-title":"Neuron"},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"108","DOI":"10.1038\/nrneurol.2011.200","article-title":"Control of autophagy as a therapy for neurodegenerative disease","volume":"8","author":"Harris","year":"2011","journal-title":"Nat. Rev. Neurol."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"660","DOI":"10.1038\/nrd.2018.109","article-title":"Promoting the clearance of neurotoxic proteins in neurodegenerative disorders of ageing","volume":"17","author":"Boland","year":"2018","journal-title":"Nat. Rev. Drug Discov."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"1263","DOI":"10.1016\/j.cell.2014.11.006","article-title":"Metabolic control of autophagy","volume":"159","author":"Galluzzi","year":"2014","journal-title":"Cell"},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"1110","DOI":"10.1038\/s41556-018-0201-5","article-title":"Life, death and autophagy","volume":"20","author":"Doherty","year":"2018","journal-title":"Nat. Cell Biol."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"803","DOI":"10.1161\/CIRCRESAHA.118.312208","article-title":"Autophagy in Cardiovascular Aging","volume":"123","author":"Abdellatif","year":"2018","journal-title":"Circ. Res."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"699","DOI":"10.1016\/j.tem.2018.08.001","article-title":"Metabolic Stress, Autophagy, and Cardiovascular Aging: From Pathophysiology to Therapeutics","volume":"29","author":"Ren","year":"2018","journal-title":"Trends Endocrinol. Metab."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"543","DOI":"10.1038\/s41569-018-0059-z","article-title":"Mitochondrial quality control mechanisms as molecular targets in cardiac ageing","volume":"15","author":"Picca","year":"2018","journal-title":"Nat. Rev. Cardiol."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1016\/j.arr.2018.08.004","article-title":"The effect of fasting or calorie restriction on autophagy induction: A review of the literature","volume":"47","author":"Bagherniya","year":"2018","journal-title":"Ageing Res. Rev."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"682","DOI":"10.1016\/j.cell.2011.07.030","article-title":"Autophagy and aging","volume":"146","author":"Rubinsztein","year":"2011","journal-title":"Cell"},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"243","DOI":"10.1080\/15548627.2017.1402992","article-title":"Autophagy balances inflammation in innate immunity","volume":"14","author":"Deretic","year":"2018","journal-title":"Autophagy"},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"224","DOI":"10.1016\/j.molcel.2014.03.009","article-title":"Autophagy in antimicrobial immunity","volume":"54","author":"Gomes","year":"2014","journal-title":"Mol. Cell"},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"356","DOI":"10.1038\/s41574-018-0009-1","article-title":"Targeting autophagy in obesity: From pathophysiology to management","volume":"14","author":"Zhang","year":"2018","journal-title":"Nat. Rev. Endocrinol."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"322","DOI":"10.1038\/nrendo.2014.35","article-title":"Autophagy\u2014A key player in cellular and body metabolism","volume":"10","author":"Kim","year":"2014","journal-title":"Nat. Rev. Endocrinol."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1172\/JCI78652","article-title":"Autophagy: A druggable process that is deregulated in aging and human disease","volume":"125","author":"Kroemer","year":"2015","journal-title":"J. Clin. Investig."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"1250256","DOI":"10.1126\/science.1250256","article-title":"Cell biology. Metabolic control of cell death","volume":"345","author":"Green","year":"2014","journal-title":"Science"},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"673","DOI":"10.4161\/auto.7.7.14733","article-title":"Microautophagy in mammalian cells: Revisiting a 40-year-old conundrum","volume":"7","author":"Mijaljica","year":"2011","journal-title":"Autophagy"},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"e1800008","DOI":"10.1002\/bies.201800008","article-title":"Three Distinct Types of Microautophagy Based on Membrane Dynamics and Molecular Machineries","volume":"40","author":"Oku","year":"2018","journal-title":"Bioessays"},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"1125","DOI":"10.1007\/s00018-011-0865-5","article-title":"Microautophagy: Lesser-known self-eating","volume":"69","author":"Li","year":"2012","journal-title":"Cell Mol. Life Sci."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"4492","DOI":"10.1091\/mbc.e08-04-0363","article-title":"Piecemeal microautophagy of the nucleus requires the core macroautophagy genes","volume":"19","author":"Krick","year":"2008","journal-title":"Mol. Biol. Cell"},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"3263","DOI":"10.1083\/jcb.201611029","article-title":"Evidence for ESCRT- and clathrin-dependent microautophagy","volume":"216","author":"Oku","year":"2017","journal-title":"J. Cell Biol."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"529","DOI":"10.1083\/jcb.151.3.529","article-title":"Cell-free reconstitution of microautophagic vacuole invagination and vesicle formation","volume":"151","author":"Sattler","year":"2000","journal-title":"J. Cell Biol."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"357","DOI":"10.1083\/jcb.201404115","article-title":"A sterol-enriched vacuolar microdomain mediates stationary phase lipophagy in budding yeast","volume":"206","author":"Wang","year":"2014","journal-title":"J. Cell Biol."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"365","DOI":"10.1038\/s41580-018-0001-6","article-title":"The coming of age of chaperone-mediated autophagy","volume":"19","author":"Kaushik","year":"2018","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"5414","DOI":"10.1074\/jbc.R117.818237","article-title":"Chaperone-mediated autophagy and endosomal microautophagy: Joint by a chaperone","volume":"293","author":"Tekirdag","year":"2018","journal-title":"J. Biol. Chem."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"6823","DOI":"10.1038\/ncomms7823","article-title":"Regulated degradation of Chk1 by chaperone-mediated autophagy in response to DNA damage","volume":"6","author":"Park","year":"2015","journal-title":"Nat. Commun."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"C1200","DOI":"10.1152\/ajpcell.1995.269.5.C1200","article-title":"Activation of a selective pathway of lysosomal proteolysis in rat liver by prolonged starvation","volume":"269","author":"Cuervo","year":"1995","journal-title":"Am. J. Physiol"},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"4829","DOI":"10.1091\/mbc.e04-06-0477","article-title":"Activation of chaperone-mediated autophagy during oxidative stress","volume":"15","author":"Kiffin","year":"2004","journal-title":"Mol. Biol. Cell"},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"431","DOI":"10.1016\/j.neuint.2012.01.020","article-title":"Hypoxic stress activates chaperone-mediated autophagy and modulates neuronal cell survival","volume":"60","author":"Dohi","year":"2012","journal-title":"Neurochem. Int."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"25864","DOI":"10.1074\/jbc.M502456200","article-title":"Ketone bodies stimulate chaperone-mediated autophagy","volume":"280","author":"Finn","year":"2005","journal-title":"J. Biol. Chem."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"1349","DOI":"10.4161\/auto.25190","article-title":"STUB1\/CHIP is required for HIF1A degradation by chaperone-mediated autophagy","volume":"9","author":"Ferreira","year":"2013","journal-title":"Autophagy"},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"417","DOI":"10.1016\/j.cmet.2014.06.009","article-title":"Deficient chaperone-mediated autophagy in liver leads to metabolic dysregulation","volume":"20","author":"Schneider","year":"2014","journal-title":"Cell Metab."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"759","DOI":"10.1038\/ncb3166","article-title":"Degradation of lipid droplet-associated proteins by chaperone-mediated autophagy facilitates lipolysis","volume":"17","author":"Kaushik","year":"2015","journal-title":"Nat. Cell Biol."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"432","DOI":"10.1080\/15548627.2015.1124226","article-title":"AMPK-dependent phosphorylation of lipid droplet protein PLIN2 triggers its degradation by CMA","volume":"12","author":"Kaushik","year":"2016","journal-title":"Autophagy"},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"1995","DOI":"10.1091\/mbc.9.8.1995","article-title":"IkappaB is a substrate for a selective pathway of lysosomal proteolysis","volume":"9","author":"Cuervo","year":"1998","journal-title":"Mol. Biol. Cell"},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"124","DOI":"10.1126\/science.1166088","article-title":"Regulation of neuronal survival factor MEF2D by chaperone-mediated autophagy","volume":"323","author":"Yang","year":"2009","journal-title":"Science"},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"1015","DOI":"10.4161\/auto.28477","article-title":"Disruption of chaperone-mediated autophagy-dependent degradation of MEF2A by oxidative stress-induced lysosome destabilization","volume":"10","author":"Zhang","year":"2014","journal-title":"Autophagy"},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"1046","DOI":"10.1038\/ni.3003","article-title":"Chaperone-mediated autophagy regulates T cell responses through targeted degradation of negative regulators of T cell activation","volume":"15","author":"Valdor","year":"2014","journal-title":"Nat. Immunol."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"555","DOI":"10.1016\/j.immuni.2016.08.014","article-title":"Sumoylation Promotes the Stability of the DNA Sensor cGAS and the Adaptor STING to Regulate the Kinetics of Response to DNA Virus","volume":"45","author":"Hu","year":"2016","journal-title":"Immunity"},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"E3325","DOI":"10.1073\/pnas.1412840111","article-title":"Cyclin-dependent kinases regulate lysosomal degradation of hypoxia-inducible factor 1alpha to promote cell-cycle progression","volume":"111","author":"Hubbi","year":"2014","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"31505","DOI":"10.1074\/jbc.M002102200","article-title":"Age-related decline in chaperone-mediated autophagy","volume":"275","author":"Cuervo","year":"2000","journal-title":"J. Biol. Chem."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"959","DOI":"10.1038\/nm.1851","article-title":"Restoration of chaperone-mediated autophagy in aging liver improves cellular maintenance and hepatic function","volume":"14","author":"Zhang","year":"2008","journal-title":"Nat. Med."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"719","DOI":"10.1016\/j.molcel.2011.04.025","article-title":"Acetylation targets the M2 isoform of pyruvate kinase for degradation through chaperone-mediated autophagy and promotes tumor growth","volume":"42","author":"Lv","year":"2011","journal-title":"Mol. Cell"},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"1643","DOI":"10.4161\/auto.21654","article-title":"LAMP2A overexpression in breast tumors promotes cancer cell survival via chaperone-mediated autophagy","volume":"8","author":"Saha","year":"2012","journal-title":"Autophagy"},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"40019","DOI":"10.18632\/oncotarget.16685","article-title":"Chaperone-mediated autophagy compensates for impaired macroautophagy in the cirrhotic liver to promote hepatocellular carcinoma","volume":"8","author":"Chava","year":"2017","journal-title":"Oncotarget"},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"2130","DOI":"10.1093\/brain\/awt131","article-title":"Boosting chaperone-mediated autophagy in vivo mitigates alpha-synuclein-induced neurodegeneration","volume":"136","author":"Xilouri","year":"2013","journal-title":"Brain"},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"1215","DOI":"10.1080\/15548627.2016.1179401","article-title":"Essential control of mitochondrial morphology and function by chaperone-mediated autophagy through degradation of PARK7","volume":"12","author":"Wang","year":"2016","journal-title":"Autophagy"},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"4153","DOI":"10.1093\/hmg\/ddp367","article-title":"Tau fragmentation, aggregation and clearance: The dual role of lysosomal processing","volume":"18","author":"Wang","year":"2009","journal-title":"Hum. Mol. Genet."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"337","DOI":"10.5483\/BMBRep.2016.49.6.212","article-title":"Regulation of amyloid precursor protein processing by its KFERQ motif","volume":"49","author":"Park","year":"2016","journal-title":"BMB Rep."},{"key":"ref_105","first-page":"3024","article-title":"Metabolism and mis-metabolism of the neuropathological signature protein TDP-43","volume":"127","author":"Huang","year":"2014","journal-title":"J. Cell Sci."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"256","DOI":"10.1038\/nbt.1608","article-title":"Harnessing chaperone-mediated autophagy for the selective degradation of mutant huntingtin protein","volume":"28","author":"Bauer","year":"2010","journal-title":"Nat. Biotechnol."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"18492","DOI":"10.1523\/JNEUROSCI.3219-11.2011","article-title":"Constitutive upregulation of chaperone-mediated autophagy in Huntington\u2019s disease","volume":"31","author":"Koga","year":"2011","journal-title":"J. Neurosci."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"544","DOI":"10.1016\/j.biopha.2017.05.037","article-title":"Inhibition of PI3K\/AKt\/mTOR signaling pathway protects against d-galactosamine\/lipopolysaccharide-induced acute liver failure by chaperone-mediated autophagy in rats","volume":"92","author":"Li","year":"2017","journal-title":"Biomed. Pharmacother."},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"G950","DOI":"10.1152\/ajpgi.00235.2013","article-title":"Purinergic receptor X7 is a key modulator of metabolic oxidative stress-mediated autophagy and inflammation in experimental nonalcoholic steatohepatitis","volume":"305","author":"Das","year":"2013","journal-title":"Am. J. Physiol. Gastrointest. Liver Physiol."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"344","DOI":"10.1002\/jcp.21676","article-title":"Chaperone-mediated autophagy is defective in mucolipidosis type IV","volume":"219","author":"Venugopal","year":"2009","journal-title":"J. Cell Physiol."},{"key":"ref_111","first-page":"193","article-title":"Membrane dynamics in autophagosome biogenesis","volume":"128","author":"Carlsson","year":"2015","journal-title":"J. Cell Sci."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"759","DOI":"10.1038\/nrm3696","article-title":"The autophagosome: Origins unknown, biogenesis complex","volume":"14","author":"Lamb","year":"2013","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1038\/cr.2013.159","article-title":"A current perspective of autophagosome biogenesis","volume":"24","author":"Shibutani","year":"2014","journal-title":"Cell Res."},{"key":"ref_114","unstructured":"Walker, S.A., and Ktistakis, N.T. (2019). Autophagosome Biogenesis Machinery. J. Mol. Biol."},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"1433","DOI":"10.1038\/ncb1991","article-title":"A subdomain of the endoplasmic reticulum forms a cradle for autophagosome formation","volume":"11","author":"Fujita","year":"2009","journal-title":"Nat. Cell Biol."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"1180","DOI":"10.4161\/auto.5.8.10274","article-title":"3D tomography reveals connections between the phagophore and endoplasmic reticulum","volume":"5","author":"Vihinen","year":"2009","journal-title":"Autophagy"},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1083\/jcb.200904075","article-title":"The conserved oligomeric Golgi complex is involved in double-membrane vesicle formation during autophagy","volume":"188","author":"Yen","year":"2010","journal-title":"J. Cell Biol."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"101","DOI":"10.4161\/auto.1.2.1840","article-title":"Atg9 cycles between mitochondria and the pre-autophagosomal structure in yeasts","volume":"1","author":"Reggiori","year":"2005","journal-title":"Autophagy"},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"747","DOI":"10.1038\/ncb2078","article-title":"Plasma membrane contributes to the formation of pre-autophagosomal structures","volume":"12","author":"Ravikumar","year":"2010","journal-title":"Nat. Cell Biol."},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"114","DOI":"10.1016\/j.devcel.2018.03.008","article-title":"The RAB11A-Positive Compartment Is a Primary Platform for Autophagosome Assembly Mediated by WIPI2 Recognition of PI3P-RAB11A","volume":"45","author":"Puri","year":"2018","journal-title":"Dev. Cell"},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1083\/jcb.201205129","article-title":"Membrane remodeling by the PX-BAR protein SNX18 promotes autophagosome formation","volume":"202","author":"Knaevelsrud","year":"2013","journal-title":"J. Cell Biol."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"389","DOI":"10.1038\/nature11910","article-title":"Autophagosomes form at ER-mitochondria contact sites","volume":"495","author":"Hamasaki","year":"2013","journal-title":"Nature"},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1016\/j.jmb.2017.01.002","article-title":"Autophagosome Maturation and Fusion","volume":"429","author":"Reggiori","year":"2017","journal-title":"J. Mol. Biol."},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"5386","DOI":"10.1074\/jbc.R117.810366","article-title":"A molecular perspective of mammalian autophagosome biogenesis","volume":"293","author":"Mercer","year":"2018","journal-title":"J. Biol. Chem."},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1016\/j.ceb.2018.04.003","article-title":"Formation and maturation of autophagosomes in higher eukaryotes: A social network","volume":"53","author":"Zhao","year":"2018","journal-title":"Curr. Opin. Cell Biol."},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"92","DOI":"10.1016\/j.ceb.2017.03.010","article-title":"The coordination of membrane fission and fusion at the end of autophagosome maturation","volume":"47","author":"Yu","year":"2017","journal-title":"Curr. Opin. Cell Biol."},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"R512","DOI":"10.1016\/j.cub.2018.02.034","article-title":"Coordination of Autophagosome-Lysosome Fusion by Atg8 Family Members","volume":"28","author":"Kriegenburg","year":"2018","journal-title":"Curr. Biol."},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1080\/15548627.2017.1378838","article-title":"Autophagy pathway: Cellular and molecular mechanisms","volume":"14","author":"Yu","year":"2018","journal-title":"Autophagy"},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"1209","DOI":"10.1242\/jcs.196352","article-title":"New insights into autophagosome-lysosome fusion","volume":"130","author":"Nakamura","year":"2017","journal-title":"J. Cell Sci."},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1146\/annurev-cellbio-092910-154005","article-title":"The role of Atg proteins in autophagosome formation","volume":"27","author":"Mizushima","year":"2011","journal-title":"Annu. Rev. Cell Dev. Biol."},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"764","DOI":"10.4161\/auto.6.6.12709","article-title":"Characterization of autophagosome formation site by a hierarchical analysis of mammalian Atg proteins","volume":"6","author":"Itakura","year":"2010","journal-title":"Autophagy"},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"361","DOI":"10.1016\/j.cell.2017.03.035","article-title":"mTOR Signaling in Growth, Metabolism, and Disease","volume":"169","author":"Saxton","year":"2017","journal-title":"Cell"},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"301","DOI":"10.1016\/j.cmet.2017.07.001","article-title":"The Dawn of the Age of Amino Acid Sensors for the mTORC1 Pathway","volume":"26","author":"Wolfson","year":"2017","journal-title":"Cell Metab."},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1038\/nrm3522","article-title":"Amino acid signalling upstream of mTOR","volume":"14","author":"Jewell","year":"2013","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"132","DOI":"10.1016\/j.ceb.2009.12.004","article-title":"The role of the Atg1\/ULK1 complex in autophagy regulation","volume":"22","author":"Mizushima","year":"2010","journal-title":"Curr. Opin. Cell Biol."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"511","DOI":"10.1083\/jcb.200911141","article-title":"Autophagy requires endoplasmic reticulum targeting of the PI3-kinase complex via Atg14L","volume":"190","author":"Matsunaga","year":"2010","journal-title":"J. Cell Biol."},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"385","DOI":"10.1038\/ncb1846","article-title":"Two Beclin 1-binding proteins, Atg14L and Rubicon, reciprocally regulate autophagy at different stages","volume":"11","author":"Matsunaga","year":"2009","journal-title":"Nat. Cell Biol."},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"741","DOI":"10.1038\/ncb2757","article-title":"ULK1 induces autophagy by phosphorylating Beclin-1 and activating VPS34 lipid kinase","volume":"15","author":"Russell","year":"2013","journal-title":"Nat. Cell Biol."},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"685","DOI":"10.1083\/jcb.200803137","article-title":"Autophagosome formation from membrane compartments enriched in phosphatidylinositol 3-phosphate and dynamically connected to the endoplasmic reticulum","volume":"182","author":"Axe","year":"2008","journal-title":"J. Cell Biol."},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"506","DOI":"10.4161\/auto.6.4.11863","article-title":"Mammalian Atg18 (WIPI2) localizes to omegasome-anchored phagophores and positively regulates LC3 lipidation","volume":"6","author":"Polson","year":"2010","journal-title":"Autophagy"},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1083\/jcb.201202061","article-title":"Atg9 vesicles are an important membrane source during early steps of autophagosome formation","volume":"198","author":"Yamamoto","year":"2012","journal-title":"J. Cell Biol."},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"1860","DOI":"10.1091\/mbc.e11-09-0746","article-title":"Dynamic and transient interactions of Atg9 with autophagosomes, but not membrane integration, are required for autophagy","volume":"23","author":"Orsi","year":"2012","journal-title":"Mol. Biol. Cell"},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"1005","DOI":"10.1083\/jcb.200912089","article-title":"An Atg9-containing compartment that functions in the early steps of autophagosome biogenesis","volume":"190","author":"Mari","year":"2010","journal-title":"J. Cell Biol."},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"1055","DOI":"10.1038\/srep01055","article-title":"The VMP1-Beclin 1 interaction regulates autophagy induction","volume":"3","author":"Molejon","year":"2013","journal-title":"Sci. Rep."},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"37124","DOI":"10.1074\/jbc.M706956200","article-title":"The pancreatitis-induced vacuole membrane protein 1 triggers autophagy in mammalian cells","volume":"282","author":"Ropolo","year":"2007","journal-title":"J. Biol. Chem."},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"974","DOI":"10.1016\/j.molcel.2017.08.005","article-title":"The ER-Localized Transmembrane Protein EPG-3\/VMP1 Regulates SERCA Activity to Control ER-Isolation Membrane Contacts for Autophagosome Formation","volume":"67","author":"Zhao","year":"2017","journal-title":"Mol. Cell"},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"33889","DOI":"10.1074\/jbc.273.51.33889","article-title":"A new protein conjugation system in human. The counterpart of the yeast Apg12p conjugation system essential for autophagy","volume":"273","author":"Mizushima","year":"1998","journal-title":"J. Biol. Chem."},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"395","DOI":"10.1038\/26506","article-title":"A protein conjugation system essential for autophagy","volume":"395","author":"Mizushima","year":"1998","journal-title":"Nature"},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"5971","DOI":"10.1093\/emboj\/20.21.5971","article-title":"The pre-autophagosomal structure organized by concerted functions of APG genes is essential for autophagosome formation","volume":"20","author":"Suzuki","year":"2001","journal-title":"EMBO J."},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1016\/j.cell.2007.05.021","article-title":"Atg8, a ubiquitin-like protein required for autophagosome formation, mediates membrane tethering and hemifusion","volume":"130","author":"Nakatogawa","year":"2007","journal-title":"Cell"},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"2092","DOI":"10.1091\/mbc.e07-12-1257","article-title":"The Atg16L complex specifies the site of LC3 lipidation for membrane biogenesis in autophagy","volume":"19","author":"Fujita","year":"2008","journal-title":"Mol. Biol. Cell"},{"key":"ref_152","doi-asserted-by":"crossref","first-page":"3888","DOI":"10.1093\/emboj\/18.14.3888","article-title":"Apg16p is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway","volume":"18","author":"Mizushima","year":"1999","journal-title":"EMBO J."},{"key":"ref_153","doi-asserted-by":"crossref","first-page":"18619","DOI":"10.1074\/jbc.M111889200","article-title":"Formation of the approximately 350-kDa Apg12-Apg5.Apg16 multimeric complex, mediated by Apg16 oligomerization, is essential for autophagy in yeast","volume":"277","author":"Kuma","year":"2002","journal-title":"J. Biol. Chem."},{"key":"ref_154","doi-asserted-by":"crossref","first-page":"5720","DOI":"10.1093\/emboj\/19.21.5720","article-title":"LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing","volume":"19","author":"Kabeya","year":"2000","journal-title":"EMBO J."},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"2805","DOI":"10.1242\/jcs.01131","article-title":"LC3, GABARAP and GATE16 localize to autophagosomal membrane depending on form-II formation","volume":"117","author":"Kabeya","year":"2004","journal-title":"J. Cell Sci."},{"key":"ref_156","doi-asserted-by":"crossref","first-page":"488","DOI":"10.1038\/35044114","article-title":"A ubiquitin-like system mediates protein lipidation","volume":"408","author":"Ichimura","year":"2000","journal-title":"Nature"},{"key":"ref_157","doi-asserted-by":"crossref","first-page":"3290","DOI":"10.1091\/mbc.e07-12-1292","article-title":"Atg8 controls phagophore expansion during autophagosome formation","volume":"19","author":"Xie","year":"2008","journal-title":"Mol. Biol. Cell"},{"key":"ref_158","doi-asserted-by":"crossref","first-page":"4304","DOI":"10.1038\/emboj.2012.278","article-title":"Mechanism and functions of membrane binding by the Atg5-Atg12\/Atg16 complex during autophagosome formation","volume":"31","author":"Romanov","year":"2012","journal-title":"EMBO J."},{"key":"ref_159","doi-asserted-by":"crossref","first-page":"37298","DOI":"10.1074\/jbc.C700195200","article-title":"The Atg12-Atg5 conjugate has a novel E3-like activity for protein lipidation in autophagy","volume":"282","author":"Hanada","year":"2007","journal-title":"J. Biol. Chem."},{"key":"ref_160","doi-asserted-by":"crossref","unstructured":"Zhen, Y., Spangenberg, H., Munson, M.J., Brech, A., Schink, K.O., Tan, K.W., Sorensen, V., Wenzel, E.M., Radulovic, M., and Engedal, N. (2019). ESCRT-mediated phagophore sealing during mitophagy. Autophagy.","DOI":"10.1080\/15548627.2019.1639301"},{"key":"ref_161","doi-asserted-by":"crossref","first-page":"3336","DOI":"10.1083\/jcb.201902170","article-title":"VPS37A directs ESCRT recruitment for phagophore closure","volume":"218","author":"Takahashi","year":"2019","journal-title":"J. Cell Biol."},{"key":"ref_162","doi-asserted-by":"crossref","first-page":"2855","DOI":"10.1038\/s41467-018-05254-w","article-title":"An autophagy assay reveals the ESCRT-III component CHMP2A as a regulator of phagophore closure","volume":"9","author":"Takahashi","year":"2018","journal-title":"Nat. Commun."},{"key":"ref_163","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1247\/csf.08005","article-title":"Dynein-dependent movement of autophagosomes mediates efficient encounters with lysosomes","volume":"33","author":"Kimura","year":"2008","journal-title":"Cell Struct. Funct."},{"key":"ref_164","doi-asserted-by":"crossref","unstructured":"Cardoso, C.M., Groth-Pedersen, L., Hoyer-Hansen, M., Kirkegaard, T., Corcelle, E., Andersen, J.S., Jaattela, M., and Nylandsted, J. (2009). Depletion of kinesin 5B affects lysosomal distribution and stability and induces peri-nuclear accumulation of autophagosomes in cancer cells. PLoS ONE, 4.","DOI":"10.1371\/journal.pone.0004424"},{"key":"ref_165","unstructured":"Lorincz, P., and Juhasz, G. (2019). Autophagosome-Lysosome Fusion. J. Mol. Biol."},{"key":"ref_166","doi-asserted-by":"crossref","first-page":"4837","DOI":"10.1242\/jcs.01370","article-title":"Role for Rab7 in maturation of late autophagic vacuoles","volume":"117","author":"Jager","year":"2004","journal-title":"J. Cell Sci."},{"key":"ref_167","doi-asserted-by":"crossref","first-page":"2687","DOI":"10.1242\/jcs.01114","article-title":"Rab7 is required for the normal progression of the autophagic pathway in mammalian cells","volume":"117","author":"Gutierrez","year":"2004","journal-title":"J. Cell Sci."},{"key":"ref_168","doi-asserted-by":"crossref","first-page":"550","DOI":"10.4161\/auto.6.4.11670","article-title":"FYCO1: Linking autophagosomes to microtubule plus end-directing molecular motors","volume":"6","author":"Pankiv","year":"2010","journal-title":"Autophagy"},{"key":"ref_169","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1083\/jcb.200907015","article-title":"FYCO1 is a Rab7 effector that binds to LC3 and PI3P to mediate microtubule plus end-directed vesicle transport","volume":"188","author":"Pankiv","year":"2010","journal-title":"J. Cell Biol."},{"key":"ref_170","doi-asserted-by":"crossref","first-page":"1680","DOI":"10.1016\/S0960-9822(01)00531-0","article-title":"The Rab7 effector protein RILP controls lysosomal transport by inducing the recruitment of dynein-dynactin motors","volume":"11","author":"Jordens","year":"2001","journal-title":"Curr. Biol."},{"key":"ref_171","doi-asserted-by":"crossref","first-page":"969","DOI":"10.1038\/emboj.2009.405","article-title":"HDAC6 controls autophagosome maturation essential for ubiquitin-selective quality-control autophagy","volume":"29","author":"Lee","year":"2010","journal-title":"EMBO J."},{"key":"ref_172","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1083\/jcb.201804165","article-title":"ATP13A2 facilitates HDAC6 recruitment to lysosome to promote autophagosome-lysosome fusion","volume":"218","author":"Wang","year":"2019","journal-title":"J. Cell Biol."},{"key":"ref_173","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1016\/j.molcel.2014.11.006","article-title":"PLEKHM1 regulates autophagosome-lysosome fusion through HOPS complex and LC3\/GABARAP proteins","volume":"57","author":"McEwan","year":"2015","journal-title":"Mol. Cell"},{"key":"ref_174","doi-asserted-by":"crossref","first-page":"e100312","DOI":"10.15252\/embj.2018100312","article-title":"Phosphatidylinositol 4,5-bisphosphate controls Rab7 and PLEKHM1 membrane cycling during autophagosome-lysosome fusion","volume":"38","author":"Baba","year":"2019","journal-title":"EMBO J."},{"key":"ref_175","doi-asserted-by":"crossref","first-page":"776","DOI":"10.1038\/ncb1740","article-title":"Beclin1-binding UVRAG targets the class C Vps complex to coordinate autophagosome maturation and endocytic trafficking","volume":"10","author":"Liang","year":"2008","journal-title":"Nat. Cell Biol."},{"key":"ref_176","doi-asserted-by":"crossref","first-page":"468","DOI":"10.1038\/ncb1854","article-title":"Distinct regulation of autophagic activity by Atg14L and Rubicon associated with Beclin 1-phosphatidylinositol-3-kinase complex","volume":"11","author":"Zhong","year":"2009","journal-title":"Nat. Cell Biol."},{"key":"ref_177","doi-asserted-by":"crossref","first-page":"365","DOI":"10.1016\/bs.mie.2016.09.065","article-title":"In Vitro Reconstitution of Autophagosome-Lysosome Fusion","volume":"587","author":"Diao","year":"2017","journal-title":"Methods Enzymol."},{"key":"ref_178","doi-asserted-by":"crossref","first-page":"563","DOI":"10.1038\/nature14147","article-title":"ATG14 promotes membrane tethering and fusion of autophagosomes to endolysosomes","volume":"520","author":"Diao","year":"2015","journal-title":"Nature"},{"key":"ref_179","doi-asserted-by":"crossref","unstructured":"Tian, X., Zheng, P., Zhou, C., Wang, X., Ma, H., Ma, W., Zhou, X., Teng, J., and Chen, J. (2019). DIPK2A promotes STX17- and VAMP7-mediated autophagosome-lysosome fusion by binding to VAMP7B. Autophagy.","DOI":"10.1080\/15548627.2019.1637199"},{"key":"ref_180","doi-asserted-by":"crossref","first-page":"1283","DOI":"10.1016\/j.chembiol.2019.07.002","article-title":"Regulation of Autophagic Flux by the 20S Proteasome","volume":"26","author":"Njomen","year":"2019","journal-title":"Cell Chem. Biol."},{"key":"ref_181","doi-asserted-by":"crossref","first-page":"857","DOI":"10.1083\/jcb.201607039","article-title":"Atg8 family LC3\/GABARAP proteins are crucial for autophagosome-lysosome fusion but not autophagosome formation during PINK1\/Parkin mitophagy and starvation","volume":"215","author":"Nguyen","year":"2016","journal-title":"J. Cell Biol."},{"key":"ref_182","doi-asserted-by":"crossref","first-page":"1787","DOI":"10.1080\/15548627.2019.1596480","article-title":"GORASP2\/GRASP55 collaborates with the PtdIns3K UVRAG complex to facilitate autophagosome-lysosome fusion","volume":"15","author":"Zhang","year":"2019","journal-title":"Autophagy"},{"key":"ref_183","doi-asserted-by":"crossref","first-page":"942","DOI":"10.1038\/nature09076","article-title":"Termination of autophagy and reformation of lysosomes regulated by mTOR","volume":"465","author":"Yu","year":"2010","journal-title":"Nature"},{"key":"ref_184","doi-asserted-by":"crossref","first-page":"924","DOI":"10.1038\/ncb2557","article-title":"Clathrin and phosphatidylinositol-4,5-bisphosphate regulate autophagic lysosome reformation","volume":"14","author":"Rong","year":"2012","journal-title":"Nat. Cell Biol."},{"key":"ref_185","doi-asserted-by":"crossref","first-page":"358","DOI":"10.1111\/tra.12484","article-title":"Recent progress in autophagic lysosome reformation","volume":"18","author":"Chen","year":"2017","journal-title":"Traffic"},{"key":"ref_186","doi-asserted-by":"crossref","first-page":"326","DOI":"10.1016\/j.devcel.2016.04.014","article-title":"Kinesin 1 Drives Autolysosome Tubulation","volume":"37","author":"Du","year":"2016","journal-title":"Dev. Cell"},{"key":"ref_187","first-page":"45","article-title":"Development of Research into Autophagic Lysosome Reformation","volume":"41","author":"Chen","year":"2018","journal-title":"Mol. Cells"},{"key":"ref_188","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1080\/15548627.2017.1386821","article-title":"Regulation of autophagic lysosome reformation by kinesin 1, clathrin and phosphatidylinositol-4,5-bisphosphate","volume":"14","author":"Liu","year":"2018","journal-title":"Autophagy"},{"key":"ref_189","doi-asserted-by":"crossref","first-page":"7826","DOI":"10.1073\/pnas.1013800108","article-title":"Spinster is required for autophagic lysosome reformation and mTOR reactivation following starvation","volume":"108","author":"Rong","year":"2011","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_190","doi-asserted-by":"crossref","first-page":"84","DOI":"10.1016\/j.molcel.2015.11.001","article-title":"Cul3-KLHL20 Ubiquitin Ligase Governs the Turnover of ULK1 and VPS34 Complexes to Control Autophagy Termination","volume":"61","author":"Liu","year":"2016","journal-title":"Mol. Cell"},{"key":"ref_191","doi-asserted-by":"crossref","first-page":"268","DOI":"10.1016\/j.molcel.2019.09.005","article-title":"A Diversity of Selective Autophagy Receptors Determines the Specificity of the Autophagy Pathway","volume":"76","author":"Kirkin","year":"2019","journal-title":"Mol. Cell"},{"key":"ref_192","doi-asserted-by":"crossref","first-page":"297","DOI":"10.1242\/jcs.13.1.297","article-title":"Intermediate cells of the pancreas. 3. Selective autophagy and destruction of beta-granules in intermediate cells of the rat pancreas induced by alloxan and streptozotocin","volume":"13","author":"Melmed","year":"1973","journal-title":"J. Cell Sci."},{"key":"ref_193","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1016\/j.jmb.2019.05.010","article-title":"History of the Selective Autophagy Research: How Did It Begin and Where Does It Stand Today?","volume":"432","author":"Kirkin","year":"2020","journal-title":"J. Mol. Biol."},{"key":"ref_194","doi-asserted-by":"crossref","first-page":"495","DOI":"10.1038\/ncb2979","article-title":"Cargo recognition and trafficking in selective autophagy","volume":"16","author":"Stolz","year":"2014","journal-title":"Nat. Cell Biol."},{"key":"ref_195","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1016\/j.molcel.2013.12.014","article-title":"Interactions between autophagy receptors and ubiquitin-like proteins form the molecular basis for selective autophagy","volume":"53","author":"Rogov","year":"2014","journal-title":"Mol. Cell"},{"key":"ref_196","doi-asserted-by":"crossref","first-page":"3237","DOI":"10.1242\/jcs.126128","article-title":"The LIR motif - crucial for selective autophagy","volume":"126","author":"Birgisdottir","year":"2013","journal-title":"J. Cell Sci."},{"key":"ref_197","doi-asserted-by":"crossref","first-page":"279","DOI":"10.4161\/auto.7.3.14487","article-title":"Selective autophagy mediated by autophagic adapter proteins","volume":"7","author":"Johansen","year":"2011","journal-title":"Autophagy"},{"key":"ref_198","doi-asserted-by":"crossref","first-page":"80","DOI":"10.1016\/j.jmb.2019.07.016","article-title":"Selective Autophagy: ATG8 Family Proteins, LIR Motifs and Cargo Receptors","volume":"432","author":"Johansen","year":"2020","journal-title":"J. Mol. Biol."},{"key":"ref_199","doi-asserted-by":"crossref","first-page":"259","DOI":"10.1016\/j.molcel.2009.04.026","article-title":"A role for ubiquitin in selective autophagy","volume":"34","author":"Kirkin","year":"2009","journal-title":"Mol. Cell"},{"key":"ref_200","doi-asserted-by":"crossref","first-page":"1382","DOI":"10.15252\/embr.201643587","article-title":"Structural and functional analysis of the GABARAP interaction motif (GIM)","volume":"18","author":"Rogov","year":"2017","journal-title":"EMBO Rep."},{"key":"ref_201","doi-asserted-by":"crossref","first-page":"978","DOI":"10.1080\/15548627.2016.1277311","article-title":"Beyond Atg8 binding: The role of AIM\/LIR motifs in autophagy","volume":"13","author":"Fracchiolla","year":"2017","journal-title":"Autophagy"},{"key":"ref_202","doi-asserted-by":"crossref","first-page":"3961","DOI":"10.1096\/fj.201600698R","article-title":"LC3\/GABARAP family proteins: Autophagy-(un)related functions","volume":"30","author":"Schaaf","year":"2016","journal-title":"FASEB J."},{"key":"ref_203","doi-asserted-by":"crossref","first-page":"1945","DOI":"10.1080\/15548627.2016.1207016","article-title":"iLIR database: A web resource for LIR motif-containing proteins in eukaryotes","volume":"12","author":"Jacomin","year":"2016","journal-title":"Autophagy"},{"key":"ref_204","doi-asserted-by":"crossref","first-page":"e18544","DOI":"10.7554\/eLife.18544","article-title":"Mechanism of cargo-directed Atg8 conjugation during selective autophagy","volume":"5","author":"Fracchiolla","year":"2016","journal-title":"Elife"},{"key":"ref_205","doi-asserted-by":"crossref","first-page":"766","DOI":"10.1016\/j.cell.2019.02.009","article-title":"ATG8-Binding UIM Proteins Define a New Class of Autophagy Adaptors and Receptors","volume":"177","author":"Marshall","year":"2019","journal-title":"Cell"},{"key":"ref_206","doi-asserted-by":"crossref","first-page":"435","DOI":"10.1083\/jcb.201402054","article-title":"Organellophagy: Eliminating cellular building blocks via selective autophagy","volume":"205","author":"Okamoto","year":"2014","journal-title":"J. Cell Biol."},{"key":"ref_207","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1038\/cdd.2012.81","article-title":"The pathways of mitophagy for quality control and clearance of mitochondria","volume":"20","author":"Ashrafi","year":"2013","journal-title":"Cell Death Differ."},{"key":"ref_208","doi-asserted-by":"crossref","first-page":"2570","DOI":"10.1128\/MCB.00166-09","article-title":"Hypoxia-induced autophagy is mediated through hypoxia-inducible factor induction of BNIP3 and BNIP3L via their BH3 domains","volume":"29","author":"Bellot","year":"2009","journal-title":"Mol. Cell Biol."},{"key":"ref_209","doi-asserted-by":"crossref","first-page":"10892","DOI":"10.1074\/jbc.M800102200","article-title":"Mitochondrial autophagy is an HIF-1-dependent adaptive metabolic response to hypoxia","volume":"283","author":"Zhang","year":"2008","journal-title":"J. Biol. Chem."},{"key":"ref_210","doi-asserted-by":"crossref","first-page":"2297","DOI":"10.1016\/j.bbamcr.2012.08.007","article-title":"Mitophagy is triggered by mild oxidative stress in a mitochondrial fission dependent manner","volume":"1823","author":"Frank","year":"2012","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_211","doi-asserted-by":"crossref","first-page":"16697","DOI":"10.1074\/jbc.M117.787739","article-title":"Reactive oxygen species trigger Parkin\/PINK1 pathway-dependent mitophagy by inducing mitochondrial recruitment of Parkin","volume":"292","author":"Xiao","year":"2017","journal-title":"J. Biol. Chem."},{"key":"ref_212","doi-asserted-by":"crossref","first-page":"e3097","DOI":"10.1038\/cddis.2017.463","article-title":"Superoxide drives progression of Parkin\/PINK1-dependent mitophagy following translocation of Parkin to mitochondria","volume":"8","author":"Xiao","year":"2017","journal-title":"Cell Death Dis."},{"key":"ref_213","doi-asserted-by":"crossref","first-page":"795","DOI":"10.1083\/jcb.200809125","article-title":"Parkin is recruited selectively to impaired mitochondria and promotes their autophagy","volume":"183","author":"Narendra","year":"2008","journal-title":"J. Cell Biol."},{"key":"ref_214","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1083\/jcb.200910140","article-title":"PINK1 stabilized by mitochondrial depolarization recruits Parkin to damaged mitochondria and activates latent Parkin for mitophagy","volume":"189","author":"Matsuda","year":"2010","journal-title":"J. Cell Biol."},{"key":"ref_215","doi-asserted-by":"crossref","unstructured":"Narendra, D.P., Jin, S.M., Tanaka, A., Suen, D.F., Gautier, C.A., Shen, J., Cookson, M.R., and Youle, R.J. (2010). PINK1 is selectively stabilized on impaired mitochondria to activate Parkin. PLoS Biol., 8.","DOI":"10.1371\/journal.pbio.1000298"},{"key":"ref_216","doi-asserted-by":"crossref","first-page":"378","DOI":"10.1073\/pnas.0911187107","article-title":"PINK1-dependent recruitment of Parkin to mitochondria in mitophagy","volume":"107","author":"Zhou","year":"2010","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_217","doi-asserted-by":"crossref","first-page":"162","DOI":"10.1038\/nature13392","article-title":"Ubiquitin is phosphorylated by PINK1 to activate parkin","volume":"510","author":"Koyano","year":"2014","journal-title":"Nature"},{"key":"ref_218","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1083\/jcb.201402104","article-title":"PINK1 phosphorylates ubiquitin to activate Parkin E3 ubiquitin ligase activity","volume":"205","author":"Kane","year":"2014","journal-title":"J. Cell Biol."},{"key":"ref_219","doi-asserted-by":"crossref","first-page":"2428","DOI":"10.1038\/ncomms3428","article-title":"Bit-by-bit autophagic removal of parkin-labelled mitochondria","volume":"4","author":"Yang","year":"2013","journal-title":"Nat. Commun."},{"key":"ref_220","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1038\/nature14893","article-title":"The ubiquitin kinase PINK1 recruits autophagy receptors to induce mitophagy","volume":"524","author":"Lazarou","year":"2015","journal-title":"Nature"},{"key":"ref_221","doi-asserted-by":"crossref","first-page":"27879","DOI":"10.1074\/jbc.M110.119537","article-title":"Nix is critical to two distinct phases of mitophagy, reactive oxygen species-mediated autophagy induction and Parkin-ubiquitin-p62-mediated mitochondrial priming","volume":"285","author":"Ding","year":"2010","journal-title":"J. Biol. Chem."},{"key":"ref_222","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1038\/embor.2009.256","article-title":"Nix is a selective autophagy receptor for mitochondrial clearance","volume":"11","author":"Novak","year":"2010","journal-title":"EMBO Rep."},{"key":"ref_223","doi-asserted-by":"crossref","first-page":"855","DOI":"10.4161\/auto.6.7.13005","article-title":"Bnip3-mediated mitochondrial autophagy is independent of the mitochondrial permeability transition pore","volume":"6","author":"Quinsay","year":"2010","journal-title":"Autophagy"},{"key":"ref_224","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1038\/ncb2422","article-title":"Mitochondrial outer-membrane protein FUNDC1 mediates hypoxia-induced mitophagy in mammalian cells","volume":"14","author":"Liu","year":"2012","journal-title":"Nat. Cell Biol."},{"key":"ref_225","doi-asserted-by":"crossref","first-page":"566","DOI":"10.1002\/embr.201438501","article-title":"ULK1 translocates to mitochondria and phosphorylates FUNDC1 to regulate mitophagy","volume":"15","author":"Wu","year":"2014","journal-title":"EMBO Rep."},{"key":"ref_226","doi-asserted-by":"crossref","first-page":"3755","DOI":"10.1038\/s41467-018-05722-3","article-title":"HUWE1 E3 ligase promotes PINK1\/PARKIN-independent mitophagy by regulating AMBRA1 activation via IKKalpha","volume":"9","author":"Peschiaroli","year":"2018","journal-title":"Nat. Commun."},{"key":"ref_227","doi-asserted-by":"crossref","first-page":"549","DOI":"10.1016\/j.cell.2014.05.048","article-title":"Autophagic clearance of polyQ proteins mediated by ubiquitin-Atg8 adaptors of the conserved CUET protein family","volume":"158","author":"Lu","year":"2014","journal-title":"Cell"},{"key":"ref_228","doi-asserted-by":"crossref","first-page":"224","DOI":"10.1016\/j.cell.2016.11.042","article-title":"Prohibitin 2 Is an Inner Mitochondrial Membrane Mitophagy Receptor","volume":"168","author":"Wei","year":"2017","journal-title":"Cell"},{"key":"ref_229","doi-asserted-by":"crossref","first-page":"375","DOI":"10.1038\/s41586-019-1667-4","article-title":"The ADP\/ATP translocase drives mitophagy independent of nucleotide exchange","volume":"575","author":"Hoshino","year":"2019","journal-title":"Nature"},{"key":"ref_230","doi-asserted-by":"crossref","first-page":"509","DOI":"10.1016\/j.devcel.2019.03.013","article-title":"NIPSNAP1 and NIPSNAP2 Act as \u201cEat Me\u201d Signals for Mitophagy","volume":"49","author":"Pankiv","year":"2019","journal-title":"Dev. Cell"},{"key":"ref_231","doi-asserted-by":"crossref","first-page":"347","DOI":"10.1016\/j.molcel.2019.02.010","article-title":"Spatiotemporal Control of ULK1 Activation by NDP52 and TBK1 during Selective Autophagy","volume":"74","author":"Vargas","year":"2019","journal-title":"Mol. Cell"},{"key":"ref_232","doi-asserted-by":"crossref","first-page":"969","DOI":"10.1038\/s41467-019-08924-5","article-title":"Omegasome-proximal PtdIns(4,5)P2 couples F-actin mediated mitoaggregate disassembly with autophagosome formation during mitophagy","volume":"10","author":"Hsieh","year":"2019","journal-title":"Nat. Commun."},{"key":"ref_233","doi-asserted-by":"crossref","first-page":"2852","DOI":"10.1038\/emboj.2012.151","article-title":"Pex3-anchored Atg36 tags peroxisomes for degradation in Saccharomyces cerevisiae","volume":"31","author":"Motley","year":"2012","journal-title":"EMBO J."},{"key":"ref_234","doi-asserted-by":"crossref","first-page":"20567","DOI":"10.1073\/pnas.0810611105","article-title":"Ubiquitin signals autophagic degradation of cytosolic proteins and peroxisomes","volume":"105","author":"Kim","year":"2008","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_235","first-page":"939","article-title":"NBR1 acts as an autophagy receptor for peroxisomes","volume":"126","author":"Deosaran","year":"2013","journal-title":"J. Cell Sci."},{"key":"ref_236","doi-asserted-by":"crossref","first-page":"4967","DOI":"10.1105\/tpc.113.116947","article-title":"Highly oxidized peroxisomes are selectively degraded via autophagy in Arabidopsis","volume":"25","author":"Shibata","year":"2013","journal-title":"Plant Cell"},{"key":"ref_237","doi-asserted-by":"crossref","first-page":"677","DOI":"10.1083\/jcb.201511034","article-title":"PEX2 is the E3 ubiquitin ligase required for pexophagy during starvation","volume":"214","author":"Sargent","year":"2016","journal-title":"J. Cell Biol."},{"key":"ref_238","doi-asserted-by":"crossref","first-page":"1259","DOI":"10.1038\/ncb3230","article-title":"ATM functions at the peroxisome to induce pexophagy in response to ROS","volume":"17","author":"Zhang","year":"2015","journal-title":"Nat. Cell Biol."},{"key":"ref_239","doi-asserted-by":"crossref","first-page":"359","DOI":"10.1038\/nature14506","article-title":"Receptor-mediated selective autophagy degrades the endoplasmic reticulum and the nucleus","volume":"522","author":"Mochida","year":"2015","journal-title":"Nature"},{"key":"ref_240","doi-asserted-by":"crossref","first-page":"354","DOI":"10.1038\/nature14498","article-title":"Regulation of endoplasmic reticulum turnover by selective autophagy","volume":"522","author":"Khaminets","year":"2015","journal-title":"Nature"},{"key":"ref_241","doi-asserted-by":"crossref","first-page":"e25555","DOI":"10.7554\/eLife.25555","article-title":"Full length RTN3 regulates turnover of tubular endoplasmic reticulum via selective autophagy","volume":"6","author":"Grumati","year":"2017","journal-title":"Elife"},{"key":"ref_242","doi-asserted-by":"crossref","first-page":"630","DOI":"10.1038\/s41418-018-0266-5","article-title":"Nucleophagy: From homeostasis to disease","volume":"26","author":"Papandreou","year":"2019","journal-title":"Cell Death Differ."},{"key":"ref_243","doi-asserted-by":"crossref","first-page":"2336","DOI":"10.1038\/emboj.2013.171","article-title":"Autophagy sequesters damaged lysosomes to control lysosomal biogenesis and kidney injury","volume":"32","author":"Maejima","year":"2013","journal-title":"EMBO J."},{"key":"ref_244","doi-asserted-by":"crossref","first-page":"2111","DOI":"10.1038\/ncomms3111","article-title":"Spatiotemporally controlled induction of autophagy-mediated lysosome turnover","volume":"4","author":"Hung","year":"2013","journal-title":"Nat. Commun."},{"key":"ref_245","doi-asserted-by":"crossref","first-page":"751","DOI":"10.1126\/science.aar2663","article-title":"NUFIP1 is a ribosome receptor for starvation-induced ribophagy","volume":"360","author":"Wyant","year":"2018","journal-title":"Science"},{"key":"ref_246","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1038\/s41556-017-0007-x","article-title":"Systematic analysis of ribophagy in human cells reveals bystander flux during selective autophagy","volume":"20","author":"An","year":"2018","journal-title":"Nat. Cell Biol."},{"key":"ref_247","doi-asserted-by":"crossref","first-page":"419","DOI":"10.1016\/j.bbrc.2009.03.039","article-title":"The MAP1-LC3 conjugation system is involved in lipid droplet formation","volume":"382","author":"Shibata","year":"2009","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_248","doi-asserted-by":"crossref","first-page":"1131","DOI":"10.1038\/nature07976","article-title":"Autophagy regulates lipid metabolism","volume":"458","author":"Singh","year":"2009","journal-title":"Nature"},{"key":"ref_249","doi-asserted-by":"crossref","first-page":"8055","DOI":"10.1128\/MCB.24.18.8055-8068.2004","article-title":"Sequestosome 1\/p62 is a polyubiquitin chain binding protein involved in ubiquitin proteasome degradation","volume":"24","author":"Seibenhener","year":"2004","journal-title":"Mol. Cell Biol."},{"key":"ref_250","doi-asserted-by":"crossref","first-page":"85","DOI":"10.4161\/auto.5172","article-title":"Parkin-mediated K63-linked polyubiquitination: A signal for targeting misfolded proteins to the aggresome-autophagy pathway","volume":"4","author":"Olzmann","year":"2008","journal-title":"Autophagy"},{"key":"ref_251","doi-asserted-by":"crossref","first-page":"1025","DOI":"10.1083\/jcb.200611128","article-title":"Parkin-mediated K63-linked polyubiquitination targets misfolded DJ-1 to aggresomes via binding to HDAC6","volume":"178","author":"Olzmann","year":"2007","journal-title":"J. Cell Biol."},{"key":"ref_252","doi-asserted-by":"crossref","first-page":"505","DOI":"10.1016\/j.molcel.2009.01.020","article-title":"A role for NBR1 in autophagosomal degradation of ubiquitinated substrates","volume":"33","author":"Kirkin","year":"2009","journal-title":"Mol. Cell"},{"key":"ref_253","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1016\/j.molcel.2010.04.007","article-title":"The selective macroautophagic degradation of aggregated proteins requires the PI3P-binding protein Alfy","volume":"38","author":"Filimonenko","year":"2010","journal-title":"Mol. Cell"},{"key":"ref_254","doi-asserted-by":"crossref","first-page":"330","DOI":"10.4161\/auto.6.3.11226","article-title":"p62\/SQSTM1 and ALFY interact to facilitate the formation of p62 bodies\/ALIS and their degradation by autophagy","volume":"6","author":"Clausen","year":"2010","journal-title":"Autophagy"},{"key":"ref_255","doi-asserted-by":"crossref","first-page":"4239","DOI":"10.1242\/jcs.01287","article-title":"Alfy, a novel FYVE-domain-containing protein associated with protein granules and autophagic membranes","volume":"117","author":"Simonsen","year":"2004","journal-title":"J. Cell Sci."},{"key":"ref_256","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1038\/nature13148","article-title":"Quantitative proteomics identifies NCOA4 as the cargo receptor mediating ferritinophagy","volume":"509","author":"Mancias","year":"2014","journal-title":"Nature"},{"key":"ref_257","doi-asserted-by":"crossref","first-page":"1425","DOI":"10.1080\/15548627.2016.1187366","article-title":"Autophagy promotes ferroptosis by degradation of ferritin","volume":"12","author":"Hou","year":"2016","journal-title":"Autophagy"},{"key":"ref_258","doi-asserted-by":"crossref","first-page":"e10308","DOI":"10.7554\/eLife.10308","article-title":"Ferritinophagy via NCOA4 is required for erythropoiesis and is regulated by iron dependent HERC2-mediated proteolysis","volume":"4","author":"Mancias","year":"2015","journal-title":"Elife"},{"key":"ref_259","doi-asserted-by":"crossref","first-page":"411","DOI":"10.1016\/j.celrep.2015.12.065","article-title":"NCOA4 Deficiency Impairs Systemic Iron Homeostasis","volume":"14","author":"Bellelli","year":"2016","journal-title":"Cell Rep."},{"key":"ref_260","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1016\/j.chom.2010.01.007","article-title":"Autophagy protects against Sindbis virus infection of the central nervous system","volume":"7","author":"Orvedahl","year":"2010","journal-title":"Cell Host Microbe"},{"key":"ref_261","doi-asserted-by":"crossref","first-page":"567","DOI":"10.1016\/j.cell.2005.03.007","article-title":"Autophagy regulates programmed cell death during the plant innate immune response","volume":"121","author":"Liu","year":"2005","journal-title":"Cell"},{"key":"ref_262","doi-asserted-by":"crossref","first-page":"8586","DOI":"10.1128\/JVI.72.11.8586-8596.1998","article-title":"Protection against fatal Sindbis virus encephalitis by beclin, a novel Bcl-2-interacting protein","volume":"72","author":"Liang","year":"1998","journal-title":"J. Virol."},{"key":"ref_263","doi-asserted-by":"crossref","first-page":"515","DOI":"10.1016\/j.chom.2015.02.008","article-title":"Autophagy receptor NDP52 regulates pathogen-containing autophagosome maturation","volume":"17","author":"Verlhac","year":"2015","journal-title":"Cell Host Microbe"},{"key":"ref_264","doi-asserted-by":"crossref","first-page":"228","DOI":"10.1126\/science.1205405","article-title":"Phosphorylation of the autophagy receptor optineurin restricts Salmonella growth","volume":"333","author":"Wild","year":"2011","journal-title":"Science"},{"key":"ref_265","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1016\/j.immuni.2012.04.015","article-title":"TBK-1 promotes autophagy-mediated antimicrobial defense by controlling autophagosome maturation","volume":"37","author":"Pilli","year":"2012","journal-title":"Immunity"},{"key":"ref_266","doi-asserted-by":"crossref","first-page":"618","DOI":"10.1016\/j.molcel.2013.08.003","article-title":"Phosphorylation of p62 activates the Keap1-Nrf2 pathway during selective autophagy","volume":"51","author":"Ichimura","year":"2013","journal-title":"Mol. Cell"},{"key":"ref_267","doi-asserted-by":"crossref","first-page":"822","DOI":"10.1016\/j.febslet.2014.01.045","article-title":"Dissection of the role of p62\/Sqstm1 in activation of Nrf2 during xenophagy","volume":"588","author":"Ishimura","year":"2014","journal-title":"FEBS Lett."},{"key":"ref_268","doi-asserted-by":"crossref","first-page":"745","DOI":"10.1038\/s41556-018-0124-1","article-title":"The multifaceted contributions of mitochondria to cellular metabolism","volume":"20","author":"Spinelli","year":"2018","journal-title":"Nat. Cell Biol."},{"key":"ref_269","doi-asserted-by":"crossref","first-page":"755","DOI":"10.1038\/s41556-018-0133-0","article-title":"Mitochondrial dynamics in adaptive and maladaptive cellular stress responses","volume":"20","author":"Eisner","year":"2018","journal-title":"Nat. Cell Biol."},{"key":"ref_270","doi-asserted-by":"crossref","first-page":"341","DOI":"10.1042\/EBC20170104","article-title":"Mitochondrial dynamics: Overview of molecular mechanisms","volume":"62","author":"Tilokani","year":"2018","journal-title":"Essays Biochem."},{"key":"ref_271","doi-asserted-by":"crossref","first-page":"1013","DOI":"10.1038\/s41556-018-0176-2","article-title":"Mechanisms of mitophagy in cellular homeostasis, physiology and pathology","volume":"20","author":"Palikaras","year":"2018","journal-title":"Nat. Cell Biol."},{"key":"ref_272","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1083\/jcb.201603039","article-title":"mito-QC illuminates mitophagy and mitochondrial architecture in vivo","volume":"214","author":"McWilliams","year":"2016","journal-title":"J. Cell Biol."},{"key":"ref_273","doi-asserted-by":"crossref","first-page":"1576","DOI":"10.1038\/nprot.2017.060","article-title":"A fluorescence-based imaging method to measure in vitro and in vivo mitophagy using mt-Keima","volume":"12","author":"Sun","year":"2017","journal-title":"Nat. Protoc."},{"key":"ref_274","doi-asserted-by":"crossref","first-page":"202","DOI":"10.1016\/j.neuint.2017.02.007","article-title":"Mitophagy in neurodegeneration and aging","volume":"109","author":"Fivenson","year":"2017","journal-title":"Neurochem. Int."},{"key":"ref_275","doi-asserted-by":"crossref","first-page":"439","DOI":"10.1016\/j.cmet.2017.12.008","article-title":"Basal Mitophagy Occurs Independently of PINK1 in Mouse Tissues of High Metabolic Demand","volume":"27","author":"McWilliams","year":"2018","journal-title":"Cell Metab."},{"key":"ref_276","doi-asserted-by":"crossref","first-page":"19500","DOI":"10.1073\/pnas.0708818104","article-title":"NIX is required for programmed mitochondrial clearance during reticulocyte maturation","volume":"104","author":"Schweers","year":"2007","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_277","doi-asserted-by":"crossref","first-page":"232","DOI":"10.1038\/nature07006","article-title":"Essential role for Nix in autophagic maturation of erythroid cells","volume":"454","author":"Sandoval","year":"2008","journal-title":"Nature"},{"key":"ref_278","doi-asserted-by":"crossref","first-page":"1162","DOI":"10.1126\/science.aad8222","article-title":"METABOLISM. Mitochondria shape cardiac metabolism","volume":"350","author":"Gottlieb","year":"2015","journal-title":"Science"},{"key":"ref_279","doi-asserted-by":"crossref","first-page":"1330","DOI":"10.18632\/aging.100976","article-title":"Mitophagy-driven mitochondrial rejuvenation regulates stem cell fate","volume":"8","author":"Cufi","year":"2016","journal-title":"Aging"},{"key":"ref_280","doi-asserted-by":"crossref","first-page":"1543","DOI":"10.1080\/15548627.2017.1338545","article-title":"BNIP3L-dependent mitophagy accounts for mitochondrial clearance during 3 factors-induced somatic cell reprogramming","volume":"13","author":"Xiang","year":"2017","journal-title":"Autophagy"},{"key":"ref_281","doi-asserted-by":"crossref","first-page":"1144","DOI":"10.1126\/science.1211878","article-title":"Postfertilization autophagy of sperm organelles prevents paternal mitochondrial DNA transmission","volume":"334","author":"Djeddi","year":"2011","journal-title":"Science"},{"key":"ref_282","doi-asserted-by":"crossref","first-page":"e17896","DOI":"10.7554\/eLife.17896","article-title":"Elimination of paternal mitochondria in mouse embryos occurs through autophagic degradation dependent on PARKIN and MUL1","volume":"5","author":"Rojansky","year":"2016","journal-title":"Elife"},{"key":"ref_283","doi-asserted-by":"crossref","first-page":"1662","DOI":"10.1038\/cr.2011.182","article-title":"Elimination of paternal mitochondria through the lysosomal degradation pathway in C. elegans","volume":"21","author":"Zhou","year":"2011","journal-title":"Cell Res."},{"key":"ref_284","doi-asserted-by":"crossref","first-page":"1141","DOI":"10.1126\/science.1210333","article-title":"Degradation of paternal mitochondria by fertilization-triggered autophagy in C. elegans embryos","volume":"334","author":"Sato","year":"2011","journal-title":"Science"},{"key":"ref_285","doi-asserted-by":"crossref","first-page":"E5261","DOI":"10.1073\/pnas.1605844113","article-title":"Autophagy and ubiquitin-proteasome system contribute to sperm mitophagy after mammalian fertilization","volume":"113","author":"Song","year":"2016","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_286","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1016\/j.ceb.2015.01.002","article-title":"PINK1\/Parkin-mediated mitophagy in mammalian cells","volume":"33","author":"Eiyama","year":"2015","journal-title":"Curr. Opin. Cell Biol."},{"key":"ref_287","doi-asserted-by":"crossref","first-page":"98","DOI":"10.1016\/j.devcel.2009.06.014","article-title":"Atg32 is a mitochondrial protein that confers selectivity during mitophagy","volume":"17","author":"Kanki","year":"2009","journal-title":"Dev. Cell"},{"key":"ref_288","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1016\/j.devcel.2009.06.013","article-title":"Mitochondria-anchored receptor Atg32 mediates degradation of mitochondria via selective autophagy","volume":"17","author":"Okamoto","year":"2009","journal-title":"Dev. Cell"},{"key":"ref_289","doi-asserted-by":"crossref","first-page":"1787","DOI":"10.1016\/j.febslet.2013.04.030","article-title":"Mitochondrial degradation during starvation is selective and temporally distinct from bulk autophagy in yeast","volume":"587","author":"Eiyama","year":"2013","journal-title":"FEBS Lett."},{"key":"ref_290","doi-asserted-by":"crossref","first-page":"349","DOI":"10.4254\/wjh.v9.i7.349","article-title":"Parkin in cancer: Mitophagy-related\/unrelated tasks","volume":"9","author":"Eid","year":"2017","journal-title":"World J. Hepatol."},{"key":"ref_291","doi-asserted-by":"crossref","first-page":"1315","DOI":"10.1038\/onc.2016.302","article-title":"Parkin and mitophagy in cancer","volume":"36","author":"Bernardini","year":"2017","journal-title":"Oncogene"},{"key":"ref_292","doi-asserted-by":"crossref","unstructured":"Fritsch, L.E., Moore, M.E., Sarraf, S.A., and Pickrell, A.M. (2019). Ubiquitin and Receptor-Dependent Mitophagy Pathways and Their Implication in Neurodegeneration. J. Mol. Biol.","DOI":"10.1016\/j.jmb.2019.10.015"},{"key":"ref_293","doi-asserted-by":"crossref","first-page":"311","DOI":"10.3389\/fnagi.2019.00311","article-title":"Dysfunctional Mitochondria and Mitophagy as Drivers of Alzheimer\u2019s Disease Pathogenesis","volume":"11","author":"Chakravorty","year":"2019","journal-title":"Front. Aging Neurosci."},{"key":"ref_294","doi-asserted-by":"crossref","unstructured":"Kulek, A.R., Anzell, A., Wider, J.M., Sanderson, T.H., and Przyklenk, K. (2020). Mitochondrial Quality Control: Role in Cardiac Models of Lethal Ischemia-Reperfusion Injury. Cells, 9.","DOI":"10.3390\/cells9010214"},{"key":"ref_295","doi-asserted-by":"crossref","first-page":"779","DOI":"10.1016\/j.kint.2015.11.021","article-title":"Autophagy in acute kidney injury","volume":"89","author":"Kaushal","year":"2016","journal-title":"Kidney Int."},{"key":"ref_296","doi-asserted-by":"crossref","first-page":"1193","DOI":"10.3389\/fphar.2019.01193","article-title":"Mitophagy in Hepatic Insulin Resistance: Therapeutic Potential and Concerns","volume":"10","author":"Su","year":"2019","journal-title":"Front. Pharmacol."},{"key":"ref_297","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1080\/15548627.2019.1603547","article-title":"Emerging views of mitophagy in immunity and autoimmune diseases","volume":"16","author":"Xu","year":"2020","journal-title":"Autophagy"},{"key":"ref_298","doi-asserted-by":"crossref","first-page":"975","DOI":"10.1016\/j.bbrc.2008.10.104","article-title":"PINK1 controls mitochondrial localization of Parkin through direct phosphorylation","volume":"377","author":"Kim","year":"2008","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_299","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1016\/j.neuron.2014.12.007","article-title":"The roles of PINK1, parkin, and mitochondrial fidelity in Parkinson\u2019s disease","volume":"85","author":"Pickrell","year":"2015","journal-title":"Neuron"},{"key":"ref_300","doi-asserted-by":"crossref","first-page":"120","DOI":"10.1016\/j.gendis.2019.01.004","article-title":"Impact of gene mutation in the development of Parkinson\u2019s disease","volume":"6","author":"Selvaraj","year":"2019","journal-title":"Genes Dis."},{"key":"ref_301","doi-asserted-by":"crossref","first-page":"896","DOI":"10.1016\/S0140-6736(14)61393-3","article-title":"Parkinson\u2019s disease","volume":"386","author":"Kalia","year":"2015","journal-title":"Lancet"},{"key":"ref_302","doi-asserted-by":"crossref","first-page":"933","DOI":"10.1083\/jcb.201008084","article-title":"Mitochondrial membrane potential regulates PINK1 import and proteolytic destabilization by PARL","volume":"191","author":"Jin","year":"2010","journal-title":"J. Cell Biol."},{"key":"ref_303","doi-asserted-by":"crossref","first-page":"856","DOI":"10.1111\/j.1471-4159.2011.07253.x","article-title":"The mitochondrial intramembrane protease PARL cleaves human Pink1 to regulate Pink1 trafficking","volume":"117","author":"Meissner","year":"2011","journal-title":"J. Neurochem."},{"key":"ref_304","doi-asserted-by":"crossref","first-page":"867","DOI":"10.1093\/hmg\/ddq526","article-title":"PINK1 cleavage at position A103 by the mitochondrial protease PARL","volume":"20","author":"Deas","year":"2011","journal-title":"Hum. Mol. Genet."},{"key":"ref_305","doi-asserted-by":"crossref","first-page":"1758","DOI":"10.4161\/auto.24633","article-title":"PINK1 is degraded through the N-end rule pathway","volume":"9","author":"Yamano","year":"2013","journal-title":"Autophagy"},{"key":"ref_306","doi-asserted-by":"crossref","first-page":"320","DOI":"10.1016\/j.devcel.2011.12.014","article-title":"Role of PINK1 binding to the TOM complex and alternate intracellular membranes in recruitment and activation of the E3 ligase Parkin","volume":"22","author":"Lazarou","year":"2012","journal-title":"Dev. Cell"},{"key":"ref_307","doi-asserted-by":"crossref","first-page":"120080","DOI":"10.1098\/rsob.120080","article-title":"PINK1 is activated by mitochondrial membrane potential depolarization and stimulates Parkin E3 ligase activity by phosphorylating Serine 65","volume":"2","author":"Kondapalli","year":"2012","journal-title":"Open Biol."},{"key":"ref_308","doi-asserted-by":"crossref","first-page":"1002","DOI":"10.1038\/srep01002","article-title":"PINK1-mediated phosphorylation of the Parkin ubiquitin-like domain primes mitochondrial translocation of Parkin and regulates mitophagy","volume":"2","author":"Imai","year":"2012","journal-title":"Sci. Rep."},{"key":"ref_309","doi-asserted-by":"crossref","first-page":"1016","DOI":"10.1038\/ncomms2016","article-title":"PINK1 autophosphorylation upon membrane potential dissipation is essential for Parkin recruitment to damaged mitochondria","volume":"3","author":"Okatsu","year":"2012","journal-title":"Nat. Commun."},{"key":"ref_310","doi-asserted-by":"crossref","first-page":"36372","DOI":"10.1074\/jbc.M113.509653","article-title":"A dimeric PINK1-containing complex on depolarized mitochondria stimulates Parkin recruitment","volume":"288","author":"Okatsu","year":"2013","journal-title":"J. Biol. Chem."},{"key":"ref_311","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1042\/BJ20140334","article-title":"Parkin is activated by PINK1-dependent phosphorylation of ubiquitin at Ser65","volume":"460","author":"Kazlauskaite","year":"2014","journal-title":"Biochem. J."},{"key":"ref_312","doi-asserted-by":"crossref","first-page":"21616","DOI":"10.1074\/jbc.M116.733410","article-title":"BNIP3 Protein Suppresses PINK1 Kinase Proteolytic Cleavage to Promote Mitophagy","volume":"291","author":"Zhang","year":"2016","journal-title":"J. Biol. Chem."},{"key":"ref_313","doi-asserted-by":"crossref","first-page":"332","DOI":"10.1080\/15548627.2015.1023047","article-title":"Mitophagy is primarily due to alternative autophagy and requires the MAPK1 and MAPK14 signaling pathways","volume":"11","author":"Hirota","year":"2015","journal-title":"Autophagy"},{"key":"ref_314","doi-asserted-by":"crossref","first-page":"e01958","DOI":"10.7554\/eLife.01958","article-title":"MUL1 acts in parallel to the PINK1\/parkin pathway in regulating mitofusin and compensates for loss of PINK1\/parkin","volume":"3","author":"Yun","year":"2014","journal-title":"Elife"},{"key":"ref_315","doi-asserted-by":"crossref","first-page":"1216","DOI":"10.1080\/15548627.2015.1017180","article-title":"Mitochondrial outer-membrane E3 ligase MUL1 ubiquitinates ULK1 and regulates selenite-induced mitophagy","volume":"11","author":"Li","year":"2015","journal-title":"Autophagy"},{"key":"ref_316","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1038\/nature10546","article-title":"Image-based genome-wide siRNA screen identifies selective autophagy factors","volume":"480","author":"Orvedahl","year":"2011","journal-title":"Nature"},{"key":"ref_317","doi-asserted-by":"crossref","first-page":"3476","DOI":"10.1093\/hmg\/ddw189","article-title":"The PINK1, synphilin-1 and SIAH-1 complex constitutes a novel mitophagy pathway","volume":"25","author":"Szargel","year":"2016","journal-title":"Hum. Mol. Genet."},{"key":"ref_318","doi-asserted-by":"crossref","first-page":"1153","DOI":"10.1091\/mbc.e12-08-0607","article-title":"Regulation of mitophagy by the Gp78 E3 ubiquitin ligase","volume":"24","author":"Fu","year":"2013","journal-title":"Mol. Biol. Cell"},{"key":"ref_319","first-page":"757","article-title":"Ubiquitin-mediated regulation of the E3 ligase GP78 by MGRN1 in trans affects mitochondrial homeostasis","volume":"129","author":"Mukherjee","year":"2016","journal-title":"J. Cell Sci."},{"key":"ref_320","doi-asserted-by":"crossref","first-page":"2846","DOI":"10.1016\/j.celrep.2017.08.087","article-title":"Parkin-Independent Mitophagy Controls Chemotherapeutic Response in Cancer Cells","volume":"20","author":"Villa","year":"2017","journal-title":"Cell Rep."},{"key":"ref_321","doi-asserted-by":"crossref","first-page":"1613","DOI":"10.1083\/jcb.201801044","article-title":"Basal mitophagy is widespread in Drosophila but minimally affected by loss of Pink1 or parkin","volume":"217","author":"Lee","year":"2018","journal-title":"J. Cell Biol."},{"key":"ref_322","doi-asserted-by":"crossref","first-page":"1201","DOI":"10.4161\/auto.5.8.9747","article-title":"Atg32 is a tag for mitochondria degradation in yeast","volume":"5","author":"Kanki","year":"2009","journal-title":"Autophagy"},{"key":"ref_323","doi-asserted-by":"crossref","first-page":"1203","DOI":"10.4161\/auto.5.8.9830","article-title":"A landmark protein essential for mitophagy: Atg32 recruits the autophagic machinery to mitochondria","volume":"5","author":"Okamoto","year":"2009","journal-title":"Autophagy"},{"key":"ref_324","doi-asserted-by":"crossref","first-page":"338","DOI":"10.1016\/j.celrep.2018.12.050","article-title":"A Mammalian Mitophagy Receptor, Bcl2-L-13, Recruits the ULK1 Complex to Induce Mitophagy","volume":"26","author":"Murakawa","year":"2019","journal-title":"Cell Rep."},{"key":"ref_325","doi-asserted-by":"crossref","first-page":"926","DOI":"10.4161\/auto.6716","article-title":"Selective mitochondrial autophagy during erythroid maturation","volume":"4","author":"Chen","year":"2008","journal-title":"Autophagy"},{"key":"ref_326","doi-asserted-by":"crossref","first-page":"354","DOI":"10.4161\/auto.5552","article-title":"NIX induces mitochondrial autophagy in reticulocytes","volume":"4","author":"Zhang","year":"2008","journal-title":"Autophagy"},{"key":"ref_327","doi-asserted-by":"crossref","first-page":"1146","DOI":"10.1016\/j.yjmcc.2009.12.004","article-title":"Bnip3 mediates permeabilization of mitochondria and release of cytochrome c via a novel mechanism","volume":"48","author":"Quinsay","year":"2010","journal-title":"J. Mol. Cell Cardiol."},{"key":"ref_328","doi-asserted-by":"crossref","first-page":"407","DOI":"10.1042\/BJ20070319","article-title":"Bnip3 mediates mitochondrial dysfunction and cell death through Bax and Bak","volume":"405","author":"Kubli","year":"2007","journal-title":"Biochem. J."},{"key":"ref_329","doi-asserted-by":"crossref","first-page":"721","DOI":"10.1038\/cdd.2010.146","article-title":"Bnip3 impairs mitochondrial bioenergetics and stimulates mitochondrial turnover","volume":"18","author":"Rikka","year":"2011","journal-title":"Cell Death Differ."},{"key":"ref_330","doi-asserted-by":"crossref","first-page":"H1924","DOI":"10.1152\/ajpheart.00368.2011","article-title":"Mitochondrial autophagy by Bnip3 involves Drp1-mediated mitochondrial fission and recruitment of Parkin in cardiac myocytes","volume":"301","author":"Lee","year":"2011","journal-title":"Am. J. Physiol. Heart Circ. Physiol."},{"key":"ref_331","doi-asserted-by":"crossref","first-page":"19094","DOI":"10.1074\/jbc.M111.322933","article-title":"Microtubule-associated protein 1 light chain 3 (LC3) interacts with Bnip3 protein to selectively remove endoplasmic reticulum and mitochondria via autophagy","volume":"287","author":"Hanna","year":"2012","journal-title":"J. Biol. Chem."},{"key":"ref_332","doi-asserted-by":"crossref","first-page":"2528","DOI":"10.1093\/hmg\/ddv017","article-title":"The mitochondrial protein BNIP3L is the substrate of PARK2 and mediates mitophagy in PINK1\/PARK2 pathway","volume":"24","author":"Gao","year":"2015","journal-title":"Hum. Mol. Genet."},{"key":"ref_333","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1038\/ncb2012","article-title":"PINK1\/Parkin-mediated mitophagy is dependent on VDAC1 and p62\/SQSTM1","volume":"12","author":"Geisler","year":"2010","journal-title":"Nat. Cell Biol."},{"key":"ref_334","doi-asserted-by":"crossref","first-page":"1090","DOI":"10.4161\/auto.6.8.13426","article-title":"p62\/SQSTM1 is required for Parkin-induced mitochondrial clustering but not mitophagy; VDAC1 is dispensable for both","volume":"6","author":"Narendra","year":"2010","journal-title":"Autophagy"},{"key":"ref_335","doi-asserted-by":"crossref","first-page":"887","DOI":"10.1111\/j.1365-2443.2010.01426.x","article-title":"p62\/SQSTM1 cooperates with Parkin for perinuclear clustering of depolarized mitochondria","volume":"15","author":"Okatsu","year":"2010","journal-title":"Genes Cells"},{"key":"ref_336","doi-asserted-by":"crossref","first-page":"689","DOI":"10.1080\/15548627.2016.1151580","article-title":"Mitophagy receptor FUNDC1 regulates mitochondrial dynamics and mitophagy","volume":"12","author":"Chen","year":"2016","journal-title":"Autophagy"},{"key":"ref_337","doi-asserted-by":"crossref","first-page":"1368","DOI":"10.15252\/embj.201593102","article-title":"FUNDC1 regulates mitochondrial dynamics at the ER-mitochondrial contact site under hypoxic conditions","volume":"35","author":"Wu","year":"2016","journal-title":"EMBO J."},{"key":"ref_338","doi-asserted-by":"crossref","first-page":"471","DOI":"10.1126\/science.1231031","article-title":"PINK1-phosphorylated mitofusin 2 is a Parkin receptor for culling damaged mitochondria","volume":"340","author":"Chen","year":"2013","journal-title":"Science"},{"key":"ref_339","doi-asserted-by":"crossref","unstructured":"Gong, G., Song, M., Csordas, G., Kelly, D.P., Matkovich, S.J., and Dorn, G.W. (2015). Parkin-mediated mitophagy directs perinatal cardiac metabolic maturation in mice. Science, 350.","DOI":"10.1126\/science.aad2459"},{"key":"ref_340","doi-asserted-by":"crossref","first-page":"E4439","DOI":"10.1073\/pnas.1405752111","article-title":"Optineurin is an autophagy receptor for damaged mitochondria in parkin-mediated mitophagy that is disrupted by an ALS-linked mutation","volume":"111","author":"Wong","year":"2014","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_341","doi-asserted-by":"crossref","first-page":"422","DOI":"10.1080\/15548627.2015.1009792","article-title":"Temporal dynamics of PARK2\/parkin and OPTN\/optineurin recruitment during the mitophagy of damaged mitochondria","volume":"11","author":"Wong","year":"2015","journal-title":"Autophagy"},{"key":"ref_342","doi-asserted-by":"crossref","first-page":"685","DOI":"10.4161\/auto.36098","article-title":"Mutations in the ubiquitin-binding domain of OPTN\/optineurin interfere with autophagy-mediated degradation of misfolded proteins by a dominant-negative mechanism","volume":"11","author":"Shen","year":"2015","journal-title":"Autophagy"},{"key":"ref_343","doi-asserted-by":"crossref","first-page":"311","DOI":"10.1038\/cr.2017.23","article-title":"PHB2\/prohibitin 2: An inner membrane mitophagy receptor","volume":"27","author":"Lahiri","year":"2017","journal-title":"Cell Res."},{"key":"ref_344","doi-asserted-by":"crossref","first-page":"419","DOI":"10.1080\/15548627.2019.1628520","article-title":"PHB2 (prohibitin 2) promotes PINK1-PRKN\/Parkin-dependent mitophagy by the PARL-PGAM5-PINK1 axis","volume":"16","author":"Yan","year":"2020","journal-title":"Autophagy"},{"key":"ref_345","doi-asserted-by":"crossref","first-page":"10249","DOI":"10.1523\/JNEUROSCI.1917-11.2011","article-title":"Parkin interacts with Ambra1 to induce mitophagy","volume":"31","author":"Cornelissen","year":"2011","journal-title":"J. Neurosci."},{"key":"ref_346","doi-asserted-by":"crossref","first-page":"517","DOI":"10.1038\/cdd.2014.190","article-title":"AMBRA1 is able to induce mitophagy via LC3 binding, regardless of PARKIN and p62\/SQSTM1","volume":"22","author":"Strappazzon","year":"2015","journal-title":"Cell Death Differ."},{"key":"ref_347","doi-asserted-by":"crossref","first-page":"1533","DOI":"10.1038\/s41467-019-09487-1","article-title":"Reversible induction of mitophagy by an optogenetic bimodular system","volume":"10","author":"Strappazzon","year":"2019","journal-title":"Nat. Commun."},{"key":"ref_348","doi-asserted-by":"crossref","first-page":"1845","DOI":"10.1080\/15548627.2019.1637642","article-title":"NIPSNAP1 and NIPSNAP2 act as \u201ceat me\u201d signals to allow sustained recruitment of autophagy receptors during mitophagy","volume":"15","author":"Abudu","year":"2019","journal-title":"Autophagy"},{"key":"ref_349","doi-asserted-by":"crossref","unstructured":"Sugo, M., Kimura, H., Arasaki, K., Amemiya, T., Hirota, N., Dohmae, N., Imai, Y., Inoshita, T., Shiba-Fukushima, K., and Hattori, N. (2018). Syntaxin 17 regulates the localization and function of PGAM5 in mitochondrial division and mitophagy. EMBO J., 37.","DOI":"10.15252\/embj.201798899"},{"key":"ref_350","doi-asserted-by":"crossref","first-page":"2059","DOI":"10.1038\/s41467-019-10096-1","article-title":"STX17 dynamically regulated by Fis1 induces mitophagy via hierarchical macroautophagic mechanism","volume":"10","author":"Xian","year":"2019","journal-title":"Nat. Commun."},{"key":"ref_351","doi-asserted-by":"crossref","unstructured":"Yamano, K., Wang, C., Sarraf, S.A., Munch, C., Kikuchi, R., Noda, N.N., Hizukuri, Y., Kanemaki, M.T., Harper, W., and Tanaka, K. (2018). Endosomal Rab cycles regulate Parkin-mediated mitophagy. Elife, 7.","DOI":"10.7554\/eLife.31326"},{"key":"ref_352","doi-asserted-by":"crossref","unstructured":"Heo, J.M., Ordureau, A., Swarup, S., Paulo, J.A., Shen, K., Sabatini, D.M., and Harper, J.W. (2018). RAB7A phosphorylation by TBK1 promotes mitophagy via the PINK-PARKIN pathway. Sci. Adv., 4.","DOI":"10.1126\/sciadv.aav0443"},{"key":"ref_353","doi-asserted-by":"crossref","first-page":"1906","DOI":"10.4161\/auto.32177","article-title":"Choline dehydrogenase interacts with SQSTM1\/p62 to recruit LC3 and stimulate mitophagy","volume":"10","author":"Park","year":"2014","journal-title":"Autophagy"},{"key":"ref_354","doi-asserted-by":"crossref","first-page":"701","DOI":"10.1016\/j.cmet.2011.04.008","article-title":"High-mobility group box 1 is essential for mitochondrial quality control","volume":"13","author":"Tang","year":"2011","journal-title":"Cell Metab."},{"key":"ref_355","doi-asserted-by":"crossref","first-page":"1256","DOI":"10.4161\/auto.7.10.16753","article-title":"Metabolic regulation by HMGB1-mediated autophagy and mitophagy","volume":"7","author":"Kang","year":"2011","journal-title":"Autophagy"},{"key":"ref_356","doi-asserted-by":"crossref","first-page":"772","DOI":"10.1080\/15548627.2017.1281492","article-title":"Autophagosome formation and cargo sequestration in the absence of LC3\/GABARAPs","volume":"13","author":"Padman","year":"2017","journal-title":"Autophagy"},{"key":"ref_357","doi-asserted-by":"crossref","unstructured":"Furuya, N., Kakuta, S., Sumiyoshi, K., Ando, M., Nonaka, R., Suzuki, A., Kazuno, S., Saiki, S., and Hattori, N. (2018). NDP52 interacts with mitochondrial RNA poly(A) polymerase to promote mitophagy. EMBO Rep., 19.","DOI":"10.15252\/embr.201846363"},{"key":"ref_358","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1016\/j.tibs.2019.08.002","article-title":"Post-translational Modifications of Key Machinery in the Control of Mitophagy","volume":"45","author":"Wang","year":"2020","journal-title":"Trends Biochem. Sci."},{"key":"ref_359","doi-asserted-by":"crossref","first-page":"989","DOI":"10.1101\/gad.262758.115","article-title":"The three \u2018P\u2019s of mitophagy: PARKIN, PINK1, and post-translational modifications","volume":"29","author":"Durcan","year":"2015","journal-title":"Genes Dev."},{"key":"ref_360","doi-asserted-by":"crossref","first-page":"1071","DOI":"10.15252\/embr.201540891","article-title":"Expanding the ubiquitin code through post-translational modification","volume":"16","author":"Herhaus","year":"2015","journal-title":"EMBO Rep."},{"key":"ref_361","doi-asserted-by":"crossref","first-page":"180108","DOI":"10.1098\/rsob.180108","article-title":"Phosphorylation of Parkin at serine 65 is essential for its activation in vivo","volume":"8","author":"McWilliams","year":"2018","journal-title":"Open Biol."},{"key":"ref_362","doi-asserted-by":"crossref","first-page":"360","DOI":"10.1016\/j.molcel.2014.09.007","article-title":"Quantitative proteomics reveal a feedforward mechanism for mitochondrial PARKIN translocation and ubiquitin chain synthesis","volume":"56","author":"Ordureau","year":"2014","journal-title":"Mol. Cell"},{"key":"ref_363","doi-asserted-by":"crossref","first-page":"2099","DOI":"10.1038\/emboj.2013.125","article-title":"Structure of the human Parkin ligase domain in an autoinhibited state","volume":"32","author":"Wauer","year":"2013","journal-title":"EMBO J."},{"key":"ref_364","doi-asserted-by":"crossref","unstructured":"Shiba-Fukushima, K., Arano, T., Matsumoto, G., Inoshita, T., Yoshida, S., Ishihama, Y., Ryu, K.Y., Nukina, N., Hattori, N., and Imai, Y. (2014). Phosphorylation of mitochondrial polyubiquitin by PINK1 promotes Parkin mitochondrial tethering. PLoS Genet., 10.","DOI":"10.1371\/journal.pgen.1004861"},{"key":"ref_365","doi-asserted-by":"crossref","first-page":"6637","DOI":"10.1073\/pnas.1506593112","article-title":"Defining roles of PARKIN and ubiquitin phosphorylation by PINK1 in mitochondrial quality control using a ubiquitin replacement strategy","volume":"112","author":"Ordureau","year":"2015","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_366","doi-asserted-by":"crossref","first-page":"307","DOI":"10.15252\/embj.201489847","article-title":"Ubiquitin Ser65 phosphorylation affects ubiquitin structure, chain assembly and hydrolysis","volume":"34","author":"Wauer","year":"2015","journal-title":"EMBO J."},{"key":"ref_367","doi-asserted-by":"crossref","first-page":"E6097","DOI":"10.1073\/pnas.1612283113","article-title":"Miro phosphorylation sites regulate Parkin recruitment and mitochondrial motility","volume":"113","author":"Shlevkov","year":"2016","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_368","doi-asserted-by":"crossref","first-page":"893","DOI":"10.1016\/j.cell.2011.10.018","article-title":"PINK1 and Parkin target Miro for phosphorylation and degradation to arrest mitochondrial motility","volume":"147","author":"Wang","year":"2011","journal-title":"Cell"},{"key":"ref_369","doi-asserted-by":"crossref","unstructured":"Safiulina, D., Kuum, M., Choubey, V., Gogichaishvili, N., Liiv, J., Hickey, M.A., Cagalinec, M., Mandel, M., Zeb, A., and Liiv, M. (2019). Miro proteins prime mitochondria for Parkin translocation and mitophagy. EMBO J., 38.","DOI":"10.15252\/embj.201899384"},{"key":"ref_370","doi-asserted-by":"crossref","first-page":"E3349","DOI":"10.1073\/pnas.1523810113","article-title":"Dynamic recruitment and activation of ALS-associated TBK1 with its target optineurin are required for efficient mitophagy","volume":"113","author":"Moore","year":"2016","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_371","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1016\/j.molcel.2015.08.016","article-title":"The PINK1-PARKIN Mitochondrial Ubiquitylation Pathway Drives a Program of OPTN\/NDP52 Recruitment and TBK1 Activation to Promote Mitophagy","volume":"60","author":"Heo","year":"2015","journal-title":"Mol. Cell"},{"key":"ref_372","doi-asserted-by":"crossref","first-page":"4039","DOI":"10.1073\/pnas.1523926113","article-title":"Phosphorylation of OPTN by TBK1 enhances its binding to Ub chains and promotes selective autophagy of damaged mitochondria","volume":"113","author":"Richter","year":"2016","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_373","doi-asserted-by":"crossref","first-page":"66","DOI":"10.1080\/15548627.2017.1391970","article-title":"Structural insights into the ubiquitin recognition by OPTN (optineurin) and its regulation by TBK1-mediated phosphorylation","volume":"14","author":"Li","year":"2018","journal-title":"Autophagy"},{"key":"ref_374","doi-asserted-by":"crossref","first-page":"4429","DOI":"10.1093\/hmg\/ddv179","article-title":"TBK1 controls autophagosomal engulfment of polyubiquitinated mitochondria through p62\/SQSTM1 phosphorylation","volume":"24","author":"Matsumoto","year":"2015","journal-title":"Hum. Mol. Genet."},{"key":"ref_375","doi-asserted-by":"crossref","unstructured":"Pollock, S.R., Schinlever, A.R., Rohani, A., Kashatus, J.A., and Kashatus, D.F. (2019). RalA and RalB relocalization to depolarized mitochondria depends on clathrin-mediated endocytosis and facilitates TBK1 activation. PLoS ONE, 14.","DOI":"10.1371\/journal.pone.0214764"},{"key":"ref_376","doi-asserted-by":"crossref","first-page":"627","DOI":"10.1016\/j.devcel.2019.06.016","article-title":"Selective Autophagy of Mitochondria on a Ubiquitin-Endoplasmic-Reticulum Platform","volume":"50","author":"Zachari","year":"2019","journal-title":"Dev. Cell"},{"key":"ref_377","doi-asserted-by":"crossref","first-page":"770","DOI":"10.1038\/s41467-020-14533-4","article-title":"TBC1D9 regulates TBK1 activation through Ca(2+) signaling in selective autophagy","volume":"11","author":"Nozawa","year":"2020","journal-title":"Nat. Commun."},{"key":"ref_378","doi-asserted-by":"crossref","first-page":"311","DOI":"10.1080\/15548627.2017.1403716","article-title":"In mammalian skeletal muscle, phosphorylation of TOMM22 by protein kinase CSNK2\/CK2 controls mitophagy","volume":"14","author":"Kravic","year":"2018","journal-title":"Autophagy"},{"key":"ref_379","doi-asserted-by":"crossref","first-page":"362","DOI":"10.1016\/j.molcel.2014.02.034","article-title":"A regulatory signaling loop comprising the PGAM5 phosphatase and CK2 controls receptor-mediated mitophagy","volume":"54","author":"Chen","year":"2014","journal-title":"Mol. Cell"},{"key":"ref_380","doi-asserted-by":"crossref","first-page":"456","DOI":"10.1126\/science.1196371","article-title":"Phosphorylation of ULK1 (hATG1) by AMP-activated protein kinase connects energy sensing to mitophagy","volume":"331","author":"Egan","year":"2011","journal-title":"Science"},{"key":"ref_381","first-page":"1488","article-title":"Structures containing Atg9A and the ULK1 complex independently target depolarized mitochondria at initial stages of Parkin-mediated mitophagy","volume":"125","author":"Itakura","year":"2012","journal-title":"J. Cell Sci."},{"key":"ref_382","doi-asserted-by":"crossref","first-page":"3579","DOI":"10.1016\/j.celrep.2018.05.064","article-title":"The PP2A-like Protein Phosphatase Ppg1 and the Far Complex Cooperatively Counteract CK2-Mediated Phosphorylation of Atg32 to Inhibit Mitophagy","volume":"23","author":"Furukawa","year":"2018","journal-title":"Cell Rep."},{"key":"ref_383","doi-asserted-by":"crossref","first-page":"2023","DOI":"10.1080\/15548627.2018.1502565","article-title":"PTEN-L puts a brake on mitophagy","volume":"14","author":"Wang","year":"2018","journal-title":"Autophagy"},{"key":"ref_384","doi-asserted-by":"crossref","first-page":"787","DOI":"10.1038\/s41422-018-0056-0","article-title":"PTEN-L is a novel protein phosphatase for ubiquitin dephosphorylation to inhibit PINK1-Parkin-mediated mitophagy","volume":"28","author":"Wang","year":"2018","journal-title":"Cell Res."},{"key":"ref_385","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1146\/annurev-biochem-060815-014922","article-title":"Ubiquitin Ligases: Structure, Function, and Regulation","volume":"86","author":"Zheng","year":"2017","journal-title":"Annu. Rev. Biochem."},{"key":"ref_386","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1146\/annurev-biochem-061516-044916","article-title":"Mechanisms of Deubiquitinase Specificity and Regulation","volume":"86","author":"Mevissen","year":"2017","journal-title":"Annu. Rev. Biochem."},{"key":"ref_387","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1038\/nrm.2017.129","article-title":"Building and decoding ubiquitin chains for mitophagy","volume":"19","author":"Harper","year":"2018","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_388","doi-asserted-by":"crossref","first-page":"372","DOI":"10.1038\/nature12043","article-title":"Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization","volume":"496","author":"Sarraf","year":"2013","journal-title":"Nature"},{"key":"ref_389","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1016\/j.molcel.2018.03.012","article-title":"Dynamics of PARKIN-Dependent Mitochondrial Ubiquitylation in Induced Neurons and Model Systems Revealed by Digital Snapshot Proteomics","volume":"70","author":"Ordureau","year":"2018","journal-title":"Mol. Cell"},{"key":"ref_390","doi-asserted-by":"crossref","unstructured":"Heo, J.M., Harper, N.J., Paulo, J.A., Li, M., Xu, Q., Coughlin, M., Elledge, S.J., and Harper, J.W. (2019). Integrated proteogenetic analysis reveals the landscape of a mitochondrial-autophagosome synapse during PARK2-dependent mitophagy. Sci. Adv., 5.","DOI":"10.1126\/sciadv.aay4624"},{"key":"ref_391","doi-asserted-by":"crossref","first-page":"1155","DOI":"10.1038\/s41418-019-0404-8","article-title":"HUWE1 controls MCL1 stability to unleash AMBRA1-induced mitophagy","volume":"27","author":"Strappazzon","year":"2019","journal-title":"Cell Death Differ."},{"key":"ref_392","doi-asserted-by":"crossref","first-page":"495","DOI":"10.15252\/embr.201643309","article-title":"Mitochondrial E3 ligase MARCH5 regulates FUNDC1 to fine-tune hypoxic mitophagy","volume":"18","author":"Chen","year":"2017","journal-title":"EMBO Rep."},{"key":"ref_393","doi-asserted-by":"crossref","first-page":"10300","DOI":"10.1074\/jbc.RA118.006302","article-title":"Parkin recruitment to impaired mitochondria for nonselective ubiquitylation is facilitated by MITOL","volume":"294","author":"Koyano","year":"2019","journal-title":"J. Biol. Chem."},{"key":"ref_394","doi-asserted-by":"crossref","first-page":"5227","DOI":"10.1093\/hmg\/ddu244","article-title":"The deubiquitinase USP15 antagonizes Parkin-mediated mitochondrial ubiquitination and mitophagy","volume":"23","author":"Cornelissen","year":"2014","journal-title":"Hum. Mol. Genet."},{"key":"ref_395","doi-asserted-by":"crossref","first-page":"370","DOI":"10.1038\/nature13418","article-title":"The mitochondrial deubiquitinase USP30 opposes parkin-mediated mitophagy","volume":"510","author":"Bingol","year":"2014","journal-title":"Nature"},{"key":"ref_396","doi-asserted-by":"crossref","first-page":"595","DOI":"10.1080\/15548627.2015.1034408","article-title":"Deubiquitinating enzymes regulate PARK2-mediated mitophagy","volume":"11","author":"Wang","year":"2015","journal-title":"Autophagy"},{"key":"ref_397","doi-asserted-by":"crossref","first-page":"920","DOI":"10.1038\/nsmb.3475","article-title":"Mechanism and regulation of the Lys6-selective deubiquitinase USP30","volume":"24","author":"Gersch","year":"2017","journal-title":"Nat. Struct. Mol. Biol."},{"key":"ref_398","doi-asserted-by":"crossref","first-page":"2473","DOI":"10.15252\/embj.201489729","article-title":"USP8 regulates mitophagy by removing K6-linked ubiquitin conjugates from parkin","volume":"33","author":"Durcan","year":"2014","journal-title":"EMBO J."},{"key":"ref_399","doi-asserted-by":"crossref","unstructured":"Chakraborty, J., von Stockum, S., Marchesan, E., Caicci, F., Ferrari, V., Rakovic, A., Klein, C., Antonini, A., Bubacco, L., and Ziviani, E. (2018). USP14 inhibition corrects an in vivo model of impaired mitophagy. EMBO Mol. Med., 10.","DOI":"10.15252\/emmm.201809014"},{"key":"ref_400","doi-asserted-by":"crossref","unstructured":"Niu, K., Fang, H., Chen, Z., Zhu, Y., Tan, Q., Wei, D., Li, Y., Balajee, A.S., and Zhao, Y. (2019). USP33 deubiquitinates PRKN\/parkin and antagonizes its role in mitophagy. Autophagy.","DOI":"10.1080\/15548627.2019.1656957"},{"key":"ref_401","doi-asserted-by":"crossref","first-page":"111641","DOI":"10.1016\/j.yexcr.2019.111641","article-title":"Ubiquitin-specific protease USP36 knockdown impairs Parkin-dependent mitophagy via downregulation of Beclin-1-associated autophagy-related ATG14L","volume":"384","author":"Geisler","year":"2019","journal-title":"Exp. Cell Res."},{"key":"ref_402","doi-asserted-by":"crossref","first-page":"849","DOI":"10.1089\/ars.2016.6662","article-title":"Loss of NAD-Dependent Protein Deacetylase Sirtuin-2 Alters Mitochondrial Protein Acetylation and Dysregulates Mitophagy","volume":"26","author":"Liu","year":"2017","journal-title":"Antioxid. Redox Signal."},{"key":"ref_403","doi-asserted-by":"crossref","first-page":"266","DOI":"10.1016\/j.ajpath.2014.09.014","article-title":"Loss of Sirt1 promotes prostatic intraepithelial neoplasia, reduces mitophagy, and delays PARK2 translocation to mitochondria","volume":"185","author":"Pestell","year":"2015","journal-title":"Am. J. Pathol."},{"key":"ref_404","first-page":"4843","article-title":"Restricted mitochondrial protein acetylation initiates mitochondrial autophagy","volume":"126","author":"Webster","year":"2013","journal-title":"J. Cell Sci."},{"key":"ref_405","doi-asserted-by":"crossref","first-page":"25034","DOI":"10.1074\/jbc.M115.677468","article-title":"Protein N-terminal Acetylation by the NatA Complex Is Critical for Selective Mitochondrial Degradation","volume":"290","author":"Eiyama","year":"2015","journal-title":"J. Biol. Chem."},{"key":"ref_406","doi-asserted-by":"crossref","first-page":"1198","DOI":"10.1016\/j.omtn.2020.01.008","article-title":"lncRNA RMST Suppressed GBM Cell Mitophagy through Enhancing FUS SUMOylation","volume":"19","author":"Liu","year":"2020","journal-title":"Mol. Ther. Nucleic Acids"},{"key":"ref_407","doi-asserted-by":"crossref","first-page":"242","DOI":"10.1007\/BF02893566","article-title":"Cellular autophagy: Glycogen segregation in early stages of a partial liver atrophy","volume":"5","author":"Pfeifer","year":"1970","journal-title":"Virchows Arch. B Cell Pathol."},{"key":"ref_408","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1007\/BF02893998","article-title":"Cellular autophagy and cell atrophy in the rat liver during long-term starvation. A quantitative morphological study with regard to diurnal variations","volume":"12","author":"Pfeifer","year":"1973","journal-title":"Virchows Arch. B Cell Pathol."},{"key":"ref_409","first-page":"145","article-title":"Cell autophagy of the liver in starvation and undernutrition","volume":"23","author":"Krustev","year":"1976","journal-title":"Bibl. Nutr. Details"},{"key":"ref_410","doi-asserted-by":"crossref","first-page":"612","DOI":"10.1007\/BF01946531","article-title":"Temperature-dependence of stress-induced hepatic autophagy","volume":"33","author":"Salas","year":"1977","journal-title":"Experientia"},{"key":"ref_411","doi-asserted-by":"crossref","first-page":"3169","DOI":"10.1073\/pnas.76.7.3169","article-title":"Glucagon-induced autophagy and proteolysis in rat liver: Mediation by selective deprivation of intracellular amino acids","volume":"76","author":"Schworer","year":"1979","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_412","first-page":"521","article-title":"Studies on cellular autophagocytosis. Cyclic AMP- and dibutyryl cyclic AMP-stimulated autophagy in rat liver","volume":"72","author":"Shelburne","year":"1973","journal-title":"Am. J. Pathol."},{"key":"ref_413","doi-asserted-by":"crossref","first-page":"1618","DOI":"10.1007\/BF02034711","article-title":"Autophagy in mouse hepatocytes induced by lysine acetylsalicylate","volume":"34","author":"Aguas","year":"1978","journal-title":"Experientia"},{"key":"ref_414","doi-asserted-by":"crossref","first-page":"14514","DOI":"10.1016\/S0021-9258(18)47825-8","article-title":"Amino acid and hormonal control of macromolecular turnover in perfused rat liver. Evidence for selective autophagy","volume":"262","author":"Lardeux","year":"1987","journal-title":"J. Biol. Chem."},{"key":"ref_415","doi-asserted-by":"crossref","first-page":"2026","DOI":"10.1002\/hep.22294","article-title":"Autophagy activation by rapamycin eliminates mouse Mallory-Denk bodies and blocks their proteasome inhibitor-mediated formation","volume":"47","author":"Harada","year":"2008","journal-title":"Hepatology"},{"key":"ref_416","doi-asserted-by":"crossref","first-page":"764","DOI":"10.1016\/j.bbadis.2008.08.008","article-title":"Mallory-Denk-bodies: Lessons from keratin-containing hepatic inclusion bodies","volume":"1782","author":"Strnad","year":"2008","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_417","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1007\/s00795-009-0476-5","article-title":"Autophagy is involved in the elimination of intracellular inclusions, Mallory-Denk bodies, in hepatocytes","volume":"43","author":"Harada","year":"2010","journal-title":"Med. Mol. Morphol."},{"key":"ref_418","doi-asserted-by":"crossref","first-page":"467","DOI":"10.1016\/j.cmet.2010.04.005","article-title":"Defective hepatic autophagy in obesity promotes ER stress and causes insulin resistance","volume":"11","author":"Yang","year":"2010","journal-title":"Cell Metab."},{"key":"ref_419","doi-asserted-by":"crossref","first-page":"G599","DOI":"10.1152\/ajpgi.00418.2015","article-title":"Hepatocellular autophagy modulates the unfolded protein response and fasting-induced steatosis in mice","volume":"311","author":"Kwanten","year":"2016","journal-title":"Am. J. Physiol. Gastrointest. Liver Physiol."},{"key":"ref_420","doi-asserted-by":"crossref","first-page":"1099","DOI":"10.4161\/auto.5.8.9825","article-title":"Roles of mitophagy and the mitochondrial permeability transition in remodeling of cultured rat hepatocytes","volume":"5","author":"Kai","year":"2009","journal-title":"Autophagy"},{"key":"ref_421","doi-asserted-by":"crossref","first-page":"C308","DOI":"10.1152\/ajpcell.00056.2010","article-title":"Mitochondrial degradation by autophagy (mitophagy) in GFP-LC3 transgenic hepatocytes during nutrient deprivation","volume":"300","author":"Kim","year":"2011","journal-title":"Am. J. Physiol. Cell Physiol."},{"key":"ref_422","doi-asserted-by":"crossref","first-page":"1804","DOI":"10.1038\/s41467-017-01969-4","article-title":"Vps34 PI 3-kinase inactivation enhances insulin sensitivity through reprogramming of mitochondrial metabolism","volume":"8","author":"Bilanges","year":"2017","journal-title":"Nat. Commun."},{"key":"ref_423","doi-asserted-by":"crossref","first-page":"26","DOI":"10.4161\/auto.3268","article-title":"Evidence for selective mitochondrial autophagy and failure in aging","volume":"3","author":"Cavallini","year":"2007","journal-title":"Autophagy"},{"key":"ref_424","doi-asserted-by":"crossref","first-page":"114","DOI":"10.1016\/0014-4800(87)90035-9","article-title":"Increased degradation in rat liver induced by antilipolytic agents: A model for studying autophagy and protein degradation in liver?","volume":"46","author":"Bergamini","year":"1987","journal-title":"Exp. Mol. Pathol."},{"key":"ref_425","doi-asserted-by":"crossref","first-page":"4035","DOI":"10.1074\/jbc.M512283200","article-title":"Excess peroxisomes are degraded by autophagic machinery in mammals","volume":"281","author":"Iwata","year":"2006","journal-title":"J. Biol. Chem."},{"key":"ref_426","doi-asserted-by":"crossref","first-page":"449","DOI":"10.1002\/(SICI)1097-0185(199704)247:4<449::AID-AR2>3.0.CO;2-M","article-title":"Inhibition of peroxisomal degradation by 3-methyladenine (3MA) in primary cultures of rat hepatocytes","volume":"247","author":"Kondo","year":"1997","journal-title":"Anat. Rec."},{"key":"ref_427","doi-asserted-by":"crossref","first-page":"96","DOI":"10.1016\/0304-4165(85)90186-2","article-title":"Effects of antilipolytic agents on rat liver peroxisomes and peroxisomal oxidative activities","volume":"839","author":"Masiello","year":"1985","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_428","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1016\/0014-5793(92)80596-9","article-title":"Autophagic degradation of peroxisomes in isolated rat hepatocytes","volume":"304","author":"Luiken","year":"1992","journal-title":"FEBS Lett."},{"key":"ref_429","first-page":"1277","article-title":"Selective autophagy of clofibrate-induced rat liver peroxisomes. Cytochemistry and immunocytochemistry on tissue specimens and on fractions obtained by Nycodenz density gradient centrifugation","volume":"46","author":"Nardacci","year":"2000","journal-title":"Cell Mol. Biol."},{"key":"ref_430","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1016\/S0232-1513(88)80030-6","article-title":"Pathology of hepatic peroxisomes in chronic hepatitis B and immunosuppression","volume":"34","author":"Reinke","year":"1988","journal-title":"Exp. Pathol."},{"key":"ref_431","doi-asserted-by":"crossref","first-page":"882","DOI":"10.1016\/j.cmet.2014.09.017","article-title":"Hif-2alpha promotes degradation of mammalian peroxisomes by selective autophagy","volume":"20","author":"Walter","year":"2014","journal-title":"Cell Metab."},{"key":"ref_432","doi-asserted-by":"crossref","first-page":"455","DOI":"10.1007\/s00418-009-0564-6","article-title":"Degradation of excess peroxisomes in mammalian liver cells by autophagy and other mechanisms","volume":"131","author":"Yokota","year":"2009","journal-title":"Histochem. Cell Biol."},{"key":"ref_433","doi-asserted-by":"crossref","first-page":"287","DOI":"10.33549\/physiolres.932285","article-title":"Autophagy-lysosomal pathway is involved in lipid degradation in rat liver","volume":"61","author":"Skop","year":"2012","journal-title":"Physiol. Res."},{"key":"ref_434","doi-asserted-by":"crossref","first-page":"234","DOI":"10.1016\/j.tem.2011.02.003","article-title":"Regulation of lipid droplets by autophagy","volume":"22","author":"Dong","year":"2011","journal-title":"Trends Endocrinol. Metab."},{"key":"ref_435","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1146\/annurev-nutr-071813-105336","article-title":"Autophagy and Lipid Droplets in the Liver","volume":"35","author":"Singh","year":"2015","journal-title":"Annu. Rev. Nutr."},{"key":"ref_436","doi-asserted-by":"crossref","first-page":"2674","DOI":"10.1091\/mbc.e05-07-0659","article-title":"Cytoplasmic lipid droplets are sites of convergence of proteasomal and autophagic degradation of apolipoprotein B","volume":"17","author":"Ohsaki","year":"2006","journal-title":"Mol. Biol. Cell"},{"key":"ref_437","doi-asserted-by":"crossref","first-page":"840","DOI":"10.1053\/j.gastro.2008.05.055","article-title":"Acute liver cell damage in patients with anorexia nervosa: A possible role of starvation-induced hepatocyte autophagy","volume":"135","author":"Rautou","year":"2008","journal-title":"Gastroenterology"},{"key":"ref_438","doi-asserted-by":"crossref","first-page":"2188","DOI":"10.1053\/j.gastro.2011.08.005","article-title":"Autophagy suppresses age-dependent ischemia and reperfusion injury in livers of mice","volume":"141","author":"Wang","year":"2011","journal-title":"Gastroenterology"},{"key":"ref_439","doi-asserted-by":"crossref","first-page":"1058","DOI":"10.1074\/jbc.274.2.1058","article-title":"Regulation of translational effectors by amino acid and mammalian target of rapamycin signaling pathways. Possible involvement of autophagy in cultured hepatoma cells","volume":"274","author":"Shigemitsu","year":"1999","journal-title":"J. Biol. Chem."},{"key":"ref_440","doi-asserted-by":"crossref","first-page":"23707","DOI":"10.1074\/jbc.272.38.23707","article-title":"Nutrient deprivation of cultured rat hepatocytes increases the desferrioxamine-available iron pool and augments the sensitivity to hydrogen peroxide","volume":"272","author":"Ollinger","year":"1997","journal-title":"J. Biol. Chem."},{"key":"ref_441","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1679\/aohc.68.71","article-title":"Participation of autophagy in the degeneration process of rat hepatocytes after transplantation following prolonged cold preservation","volume":"68","author":"Lu","year":"2005","journal-title":"Arch. Histol. Cytol."},{"key":"ref_442","doi-asserted-by":"crossref","first-page":"258","DOI":"10.4161\/auto.2882","article-title":"The role of autophagy in alpha-1-antitrypsin deficiency: A specific cellular response in genetic diseases associated with aggregation-prone proteins","volume":"2","author":"Perlmutter","year":"2006","journal-title":"Autophagy"},{"key":"ref_443","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1038\/cdd.2008.103","article-title":"Autophagic disposal of the aggregation-prone protein that causes liver inflammation and carcinogenesis in alpha-1-antitrypsin deficiency","volume":"16","author":"Perlmutter","year":"2009","journal-title":"Cell Death Differ."},{"key":"ref_444","doi-asserted-by":"crossref","first-page":"1579","DOI":"10.1172\/JCI0216787","article-title":"Liver injury in alpha1-antitrypsin deficiency: An aggregated protein induces mitochondrial injury","volume":"110","author":"Perlmutter","year":"2002","journal-title":"J. Clin. Investig."},{"key":"ref_445","doi-asserted-by":"crossref","first-page":"1228","DOI":"10.1002\/hep.21822","article-title":"Alpha-1-antitrypsin mutant Z protein content in individual hepatocytes correlates with cell death in a mouse model","volume":"46","author":"Lindblad","year":"2007","journal-title":"Hepatology"},{"key":"ref_446","doi-asserted-by":"crossref","first-page":"1740","DOI":"10.1053\/j.gastro.2010.07.041","article-title":"Autophagy reduces acute ethanol-induced hepatotoxicity and steatosis in mice","volume":"139","author":"Ding","year":"2010","journal-title":"Gastroenterology"},{"key":"ref_447","doi-asserted-by":"crossref","first-page":"116","DOI":"10.1016\/j.bbrc.2010.09.127","article-title":"CYP2E1 enhances ethanol-induced lipid accumulation but impairs autophagy in HepG2 E47 cells","volume":"402","author":"Wu","year":"2010","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_448","doi-asserted-by":"crossref","unstructured":"Sharma, S., Mells, J.E., Fu, P.P., Saxena, N.K., and Anania, F.A. (2011). GLP-1 analogs reduce hepatocyte steatosis and improve survival by enhancing the unfolded protein response and promoting macroautophagy. PLoS ONE, 6.","DOI":"10.1371\/journal.pone.0025269"},{"key":"ref_449","doi-asserted-by":"crossref","first-page":"487","DOI":"10.1124\/jpet.111.184341","article-title":"Differential roles of unsaturated and saturated fatty acids on autophagy and apoptosis in hepatocytes","volume":"339","author":"Mei","year":"2011","journal-title":"J. Pharmacol. Exp. Ther."},{"key":"ref_450","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1083\/jcb.201102031","article-title":"Persistent activation of Nrf2 through p62 in hepatocellular carcinoma cells","volume":"193","author":"Inami","year":"2011","journal-title":"J. Cell Biol."},{"key":"ref_451","doi-asserted-by":"crossref","first-page":"795","DOI":"10.1101\/gad.2016211","article-title":"Autophagy-deficient mice develop multiple liver tumors","volume":"25","author":"Takamura","year":"2011","journal-title":"Genes Dev."},{"key":"ref_452","doi-asserted-by":"crossref","first-page":"12030","DOI":"10.1038\/ncomms12030","article-title":"p62\/Sqstm1 promotes malignancy of HCV-positive hepatocellular carcinoma through Nrf2-dependent metabolic reprogramming","volume":"7","author":"Saito","year":"2016","journal-title":"Nat. Commun."},{"key":"ref_453","doi-asserted-by":"crossref","first-page":"935","DOI":"10.1016\/j.ccell.2016.04.006","article-title":"p62, Upregulated during Preneoplasia, Induces Hepatocellular Carcinogenesis by Maintaining Survival of Stressed HCC-Initiating Cells","volume":"29","author":"Umemura","year":"2016","journal-title":"Cancer Cell"},{"key":"ref_454","doi-asserted-by":"crossref","first-page":"548","DOI":"10.4161\/auto.6.4.11669","article-title":"Autophagy by hepatitis B virus and for hepatitis B virus","volume":"6","author":"Sir","year":"2010","journal-title":"Autophagy"},{"key":"ref_455","doi-asserted-by":"crossref","first-page":"4383","DOI":"10.1073\/pnas.0911373107","article-title":"The early autophagic pathway is activated by hepatitis B virus and required for viral DNA replication","volume":"107","author":"Sir","year":"2010","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_456","doi-asserted-by":"crossref","first-page":"13453","DOI":"10.1128\/JVI.06064-11","article-title":"Autophagy required for hepatitis B virus replication in transgenic mice","volume":"85","author":"Tian","year":"2011","journal-title":"J. Virol."},{"key":"ref_457","doi-asserted-by":"crossref","first-page":"2241","DOI":"10.1128\/JVI.02093-07","article-title":"Hepatitis C virus genotype 1a growth and induction of autophagy","volume":"82","author":"Kanda","year":"2008","journal-title":"J. Virol."},{"key":"ref_458","doi-asserted-by":"crossref","first-page":"1054","DOI":"10.1002\/hep.22464","article-title":"Induction of incomplete autophagic response by hepatitis C virus via the unfolded protein response","volume":"48","author":"Sir","year":"2008","journal-title":"Hepatology"},{"key":"ref_459","doi-asserted-by":"crossref","first-page":"14046","DOI":"10.1073\/pnas.0907344106","article-title":"The autophagy machinery is required to initiate hepatitis C virus replication","volume":"106","author":"Dreux","year":"2009","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_460","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1172\/JCI41474","article-title":"Activation of the unfolded protein response and autophagy after hepatitis C virus infection suppresses innate antiviral immunity in vitro","volume":"121","author":"Ke","year":"2011","journal-title":"J. Clin. Investig."},{"key":"ref_461","doi-asserted-by":"crossref","first-page":"478","DOI":"10.1083\/jcb.18.2.478","article-title":"Cytolysomes in Metabolically Active Cells","volume":"18","author":"Napolitano","year":"1963","journal-title":"J. Cell Biol."},{"key":"ref_462","doi-asserted-by":"crossref","first-page":"473","DOI":"10.1083\/jcb.48.3.473","article-title":"Quantitative characterization of dense body, autophagic vacuole, and acid phosphatase-bearing particle populations during the early phases of glucagon-induced autophagy in rat liver","volume":"48","author":"Deter","year":"1971","journal-title":"J. Cell Biol."},{"key":"ref_463","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1002\/path.1711160302","article-title":"An electron-microscope study of the mode of cell death induced by cancer-chemotherapeutic agents in populations of proliferating normal and neoplastic cells","volume":"116","author":"Searle","year":"1975","journal-title":"J. Pathol."},{"key":"ref_464","doi-asserted-by":"crossref","first-page":"122","DOI":"10.1016\/0014-4827(75)90538-8","article-title":"Analog modeling of glucagon-induced autophagy in rat liver. I. Conceptual and mathematical model of telolysosome-autophagosome-autolysosome interaction","volume":"94","author":"Deter","year":"1975","journal-title":"Exp. Cell Res."},{"key":"ref_465","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1016\/0014-4827(75)90539-X","article-title":"Analog modeling of glucagon-induced autophagy in rat liver. II. Evaluation of iron labeling as a means for identifying telolysosome, autophagosome and autolysosome populations","volume":"94","author":"Deter","year":"1975","journal-title":"Exp. Cell Res."},{"key":"ref_466","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1016\/0006-291X(79)91661-9","article-title":"Alteration of lysosomal density by sequestered glycogen during deprivation-induced autophagy in rat liver","volume":"87","author":"Schworer","year":"1979","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_467","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1042\/bj1860071","article-title":"Protein degradation in hepatocyte monolayers. Effects of glucagon, adenosine 3\u2032:5\u2032-cyclic monophosphate and insulin","volume":"186","author":"Hopgood","year":"1980","journal-title":"Biochem. J."},{"key":"ref_468","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1016\/0304-4165(80)90141-5","article-title":"Amino acid inhibition of the autophagic\/lysosomal pathway of protein degradation in isolated rat hepatocytes","volume":"630","author":"Seglen","year":"1980","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_469","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1016\/0014-4827(80)90065-8","article-title":"Autophagic degradation in rat liver after vinblastine treatment","volume":"128","author":"Marzella","year":"1980","journal-title":"Exp. Cell Res."},{"key":"ref_470","doi-asserted-by":"crossref","first-page":"144","DOI":"10.1083\/jcb.93.1.144","article-title":"Isolation of autophagic vacuoles from rat liver: Morphological and biochemical characterization","volume":"93","author":"Marzella","year":"1982","journal-title":"J. Cell Biol."},{"key":"ref_471","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1042\/bj3350217","article-title":"Purification and characterization of autophagosomes from rat hepatocytes","volume":"335","author":"Stromhaug","year":"1998","journal-title":"Biochem. J."},{"key":"ref_472","doi-asserted-by":"crossref","first-page":"542","DOI":"10.4161\/auto.6.4.11272","article-title":"Purification of autophagosomes from rat hepatocytes","volume":"6","author":"Seglen","year":"2010","journal-title":"Autophagy"},{"key":"ref_473","doi-asserted-by":"crossref","first-page":"182","DOI":"10.1016\/0014-5793(87)80444-1","article-title":"Differences in the half-lives of some mitochondrial rat liver enzymes may derive partially from hepatocyte heterogeneity","volume":"224","author":"Vargas","year":"1987","journal-title":"FEBS Lett."},{"key":"ref_474","doi-asserted-by":"crossref","first-page":"621","DOI":"10.1042\/bj2510621","article-title":"Effect of streptozotocin-diabetes on rat liver mitochondrial adenosine triphosphatase turnover","volume":"251","author":"Jorda","year":"1988","journal-title":"Biochem. J."},{"key":"ref_475","doi-asserted-by":"crossref","first-page":"1433","DOI":"10.1177\/36.11.3171166","article-title":"Autophagy of mitochondria in rat liver assessed by immunogold procedures","volume":"36","author":"Knecht","year":"1988","journal-title":"J. Histochem. Cytochem."},{"key":"ref_476","first-page":"112","article-title":"Decree No. 2006. partially amending Decree No. 1906 of 30 December 1987, published in La Gaceta Oficial of the same date, 18 February 1988","volume":"15","author":"Venezuela","year":"1988","journal-title":"Annu. Rev. Popul. Law"},{"key":"ref_477","doi-asserted-by":"crossref","first-page":"G851","DOI":"10.1152\/ajpgi.00175.2003","article-title":"Mitochondrial autophagy and injury in the liver in alpha 1-antitrypsin deficiency","volume":"286","author":"Teckman","year":"2004","journal-title":"Am. J. Physiol. Gastrointest. Liver Physiol."},{"key":"ref_478","doi-asserted-by":"crossref","first-page":"G1156","DOI":"10.1152\/ajpgi.00041.2002","article-title":"Fasting in alpha1-antitrypsin deficient liver: Constitutive [correction of consultative] activation of autophagy","volume":"283","author":"Teckman","year":"2002","journal-title":"Am. J. Physiol. Gastrointest. Liver Physiol."},{"key":"ref_479","doi-asserted-by":"crossref","first-page":"408","DOI":"10.1089\/rej.2006.9.408","article-title":"Stimulation of macroautophagy can rescue older cells from 8-OHdG mtDNA accumulation: A safe and easy way to meet goals in the SENS agenda","volume":"9","author":"Donati","year":"2006","journal-title":"Rejuvenat. Res."},{"key":"ref_480","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1083\/jcb.200412022","article-title":"Impairment of starvation-induced and constitutive autophagy in Atg7-deficient mice","volume":"169","author":"Komatsu","year":"2005","journal-title":"J. Cell Biol."},{"key":"ref_481","doi-asserted-by":"crossref","first-page":"2570","DOI":"10.1128\/MCB.00167-12","article-title":"BNip3 regulates mitochondrial function and lipid metabolism in the liver","volume":"32","author":"Glick","year":"2012","journal-title":"Mol. Cell Biol."},{"key":"ref_482","doi-asserted-by":"crossref","first-page":"1725","DOI":"10.1002\/hep.22187","article-title":"Impaired autophagy: A mechanism of mitochondrial dysfunction in anoxic rat hepatocytes","volume":"47","author":"Kim","year":"2008","journal-title":"Hepatology"},{"key":"ref_483","doi-asserted-by":"crossref","first-page":"1902","DOI":"10.18632\/aging.101511","article-title":"Aging aggravates hepatic ischemia-reperfusion injury in mice by impairing mitophagy with the involvement of the EIF2alpha-parkin pathway","volume":"10","author":"Li","year":"2018","journal-title":"Aging"},{"key":"ref_484","doi-asserted-by":"crossref","first-page":"G324","DOI":"10.1152\/ajpgi.00108.2015","article-title":"Parkin regulates mitophagy and mitochondrial function to protect against alcohol-induced liver injury and steatosis in mice","volume":"309","author":"Williams","year":"2015","journal-title":"Am. J. Physiol. Gastrointest. Liver Physiol."},{"key":"ref_485","doi-asserted-by":"crossref","first-page":"G515","DOI":"10.1152\/ajpgi.00264.2015","article-title":"Mitophagy, mitochondrial spheroids, and mitochondrial-derived vesicles in alcohol-induced liver injury","volume":"309","author":"Williams","year":"2015","journal-title":"Am. J. Physiol. Gastrointest. Liver Physiol."},{"key":"ref_486","doi-asserted-by":"crossref","first-page":"G513","DOI":"10.1152\/ajpgi.00254.2015","article-title":"Mitophagy in steatotic hepatocytes of ethanol-treated wild-type and Parkin knockout mice","volume":"309","author":"Eid","year":"2015","journal-title":"Am. J. Physiol. Gastrointest. Liver Physiol."},{"key":"ref_487","doi-asserted-by":"crossref","first-page":"1402","DOI":"10.4161\/auto.7.11.17653","article-title":"Autophagy as a rescue mechanism in efavirenz-induced mitochondrial dysfunction: A lesson from hepatic cells","volume":"7","author":"Apostolova","year":"2011","journal-title":"Autophagy"},{"key":"ref_488","doi-asserted-by":"crossref","first-page":"1009","DOI":"10.1002\/hep.24459","article-title":"Compromising mitochondrial function with the antiretroviral drug efavirenz induces cell survival-promoting autophagy","volume":"54","author":"Apostolova","year":"2011","journal-title":"Hepatology"},{"key":"ref_489","doi-asserted-by":"crossref","first-page":"1780","DOI":"10.4161\/auto.25665","article-title":"Dynamin 1-like-dependent mitochondrial fission initiates overactive mitophagy in the hepatotoxicity of cadmium","volume":"9","author":"Pi","year":"2013","journal-title":"Autophagy"},{"key":"ref_490","doi-asserted-by":"crossref","first-page":"222","DOI":"10.1002\/hep.24690","article-title":"Activation of autophagy protects against acetaminophen-induced hepatotoxicity","volume":"55","author":"Ni","year":"2012","journal-title":"Hepatology"},{"key":"ref_491","doi-asserted-by":"crossref","first-page":"825","DOI":"10.1016\/j.jhep.2014.05.033","article-title":"Adiponectin protects against acetaminophen-induced mitochondrial dysfunction and acute liver injury by promoting autophagy in mice","volume":"61","author":"Lin","year":"2014","journal-title":"J. Hepatol."},{"key":"ref_492","doi-asserted-by":"crossref","first-page":"10934","DOI":"10.1074\/jbc.M114.602284","article-title":"Chronic Deletion and Acute Knockdown of Parkin Have Differential Responses to Acetaminophen-induced Mitophagy and Liver Injury in Mice","volume":"290","author":"Williams","year":"2015","journal-title":"J. Biol. Chem."},{"key":"ref_493","doi-asserted-by":"crossref","first-page":"101148","DOI":"10.1016\/j.redox.2019.101148","article-title":"Double deletion of PINK1 and Parkin impairs hepatic mitophagy and exacerbates acetaminophen-induced liver injury in mice","volume":"22","author":"Wang","year":"2019","journal-title":"Redox Biol."},{"key":"ref_494","doi-asserted-by":"crossref","unstructured":"Kang, S.W., Haydar, G., Taniane, C., Farrell, G., Arias, I.M., Lippincott-Schwartz, J., and Fu, D. (2016). AMPK Activation Prevents and Reverses Drug-Induced Mitochondrial and Hepatocyte Injury by Promoting Mitochondrial Fusion and Function. PLoS ONE, 11.","DOI":"10.1371\/journal.pone.0165638"},{"key":"ref_495","doi-asserted-by":"crossref","first-page":"113643","DOI":"10.1016\/j.bcp.2019.113643","article-title":"Mitophagy protects against acetaminophen-induced acute liver injury in mice through inhibiting NLRP3 inflammasome activation","volume":"169","author":"Shan","year":"2019","journal-title":"Biochem. Pharmacol."},{"key":"ref_496","doi-asserted-by":"crossref","first-page":"1585","DOI":"10.1172\/JCI0216782","article-title":"Alpha1-antitrypsin polymerization and the serpinopathies: Pathobiology and prospects for therapy","volume":"110","author":"Lomas","year":"2002","journal-title":"J. Clin. Investig."},{"key":"ref_497","doi-asserted-by":"crossref","first-page":"8951","DOI":"10.1021\/bi00449a001","article-title":"Implications of the three-dimensional structure of alpha 1-antitrypsin for structure and function of serpins","volume":"28","author":"Huber","year":"1989","journal-title":"Biochemistry"},{"key":"ref_498","first-page":"1504","article-title":"Molecular pathogenesis of liver disease in alpha1-antitrypsin deficiency","volume":"24","author":"Teckman","year":"1996","journal-title":"Hepatology"},{"key":"ref_499","doi-asserted-by":"crossref","first-page":"16051","DOI":"10.1038\/nrdp.2016.51","article-title":"alpha1-Antitrypsin deficiency","volume":"2","author":"Greene","year":"2016","journal-title":"Nat. Rev. Dis. Primers"},{"key":"ref_500","doi-asserted-by":"crossref","first-page":"413","DOI":"10.1016\/j.jhep.2016.03.010","article-title":"Update on alpha-1 antitrypsin deficiency: New therapies","volume":"65","author":"Lomas","year":"2016","journal-title":"J. Hepatol."},{"key":"ref_501","doi-asserted-by":"crossref","first-page":"514","DOI":"10.1002\/hep.20815","article-title":"Alpha-1-antitrypsin deficiency: A new paradigm for hepatocellular carcinoma in genetic liver disease","volume":"42","author":"Rudnick","year":"2005","journal-title":"Hepatology"},{"key":"ref_502","doi-asserted-by":"crossref","first-page":"15696","DOI":"10.1016\/S0021-9258(19)84888-3","article-title":"Elevated synthesis of human alpha 1-antitrypsin hinders the secretion of murine alpha 1-antitrypsin from hepatocytes of transgenic mice","volume":"264","author":"Sifers","year":"1989","journal-title":"J. Biol. Chem."},{"key":"ref_503","doi-asserted-by":"crossref","first-page":"1183","DOI":"10.1172\/JCI113999","article-title":"Accumulation of PiZ alpha 1-antitrypsin causes liver damage in transgenic mice","volume":"83","author":"Carlson","year":"1989","journal-title":"J. Clin. Investig."},{"key":"ref_504","first-page":"39","article-title":"Alpha1-antitrypsin deficiency: Liver disease associated with retention of a mutant secretory glycoprotein in the endoplasmic reticulum","volume":"232","author":"Perlmutter","year":"2003","journal-title":"Methods Mol. Biol."},{"key":"ref_505","doi-asserted-by":"crossref","first-page":"4467","DOI":"10.1074\/jbc.M509409200","article-title":"Intracellular inclusions containing mutant alpha1-antitrypsin Z are propagated in the absence of autophagic activity","volume":"281","author":"Kamimoto","year":"2006","journal-title":"J. Biol. Chem."},{"key":"ref_506","doi-asserted-by":"crossref","first-page":"G961","DOI":"10.1152\/ajpgi.2000.279.5.G961","article-title":"Retention of mutant alpha(1)-antitrypsin Z in endoplasmic reticulum is associated with an autophagic response","volume":"279","author":"Teckman","year":"2000","journal-title":"Am. J. Physiol. Gastrointest. Liver Physiol."},{"key":"ref_507","doi-asserted-by":"crossref","first-page":"1863","DOI":"10.1056\/NEJMcibr1008007","article-title":"Alpha1-antitrypsin deficiency and autophagy","volume":"363","author":"Marciniak","year":"2010","journal-title":"N. Engl. J. Med."},{"key":"ref_508","doi-asserted-by":"crossref","first-page":"203","DOI":"10.1091\/mbc.e04-09-0779","article-title":"Characterization of an ERAD gene as VPS30\/ATG6 reveals two alternative and functionally distinct protein quality control pathways: One for soluble Z variant of human alpha-1 proteinase inhibitor (A1PiZ) and another for aggregates of A1PiZ","volume":"17","author":"Kruse","year":"2006","journal-title":"Mol. Biol. Cell"},{"key":"ref_509","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1126\/science.1190354","article-title":"An autophagy-enhancing drug promotes degradation of mutant alpha1-antitrypsin Z and reduces hepatic fibrosis","volume":"329","author":"Hidvegi","year":"2010","journal-title":"Science"},{"key":"ref_510","doi-asserted-by":"crossref","first-page":"700","DOI":"10.1258\/ebm.2010.009297","article-title":"Rapamycin reduces intrahepatic alpha-1-antitrypsin mutant Z protein polymers and liver injury in a mouse model","volume":"235","author":"Kaushal","year":"2010","journal-title":"Exp. Biol. Med."},{"key":"ref_511","doi-asserted-by":"crossref","first-page":"1591","DOI":"10.1002\/hep.26930","article-title":"Inhibition of Niemann-Pick-type C1-like1 by ezetimibe activates autophagy in human hepatocytes and reduces mutant alpha1-antitrypsin Z deposition","volume":"59","author":"Yamamura","year":"2014","journal-title":"Hepatology"},{"key":"ref_512","doi-asserted-by":"crossref","unstructured":"Wang, Y., Cobanoglu, M.C., Li, J., Hidvegi, T., Hale, P., Ewing, M., Chu, A.S., Gong, Z., Muzumdar, R., and Pak, S.C. (2019). An analog of glibenclamide selectively enhances autophagic degradation of misfolded alpha1-antitrypsin Z. PLoS ONE, 14.","DOI":"10.1371\/journal.pone.0209748"},{"key":"ref_513","doi-asserted-by":"crossref","first-page":"279","DOI":"10.1038\/cdd.2015.96","article-title":"Sirtuin 1 suppresses mitochondrial dysfunction of ischemic mouse livers in a mitofusin 2-dependent manner","volume":"23","author":"Biel","year":"2016","journal-title":"Cell Death Differ."},{"key":"ref_514","doi-asserted-by":"crossref","unstructured":"Chun, S.K., Lee, S., Flores-Toro, J.U.R.Y., Yang, M.J., Go, K.L., Biel, T.G., Miney, C.E., Pierre Louis, S., Law, B.K., and Law, M.E. (2018). Loss of sirtuin 1 and mitofusin 2 contributes to enhanced ischemia\/reperfusion injury in aged livers. Aging Cell, 17.","DOI":"10.1111\/acel.12761"},{"key":"ref_515","first-page":"5663","article-title":"Parkin deficiency elevates hepatic ischemia\/reperfusion injury accompanying decreased mitochondrial autophagy, increased apoptosis, impaired DNA damage repair and altered cell cycle distribution","volume":"18","author":"Ning","year":"2018","journal-title":"Mol. Med. Rep."},{"key":"ref_516","doi-asserted-by":"crossref","first-page":"94","DOI":"10.1016\/j.lfs.2018.03.017","article-title":"Heme oxygenase-1 protects liver against ischemia\/reperfusion injury via phosphoglycerate mutase family member 5-mediated mitochondrial quality control","volume":"200","author":"Hong","year":"2018","journal-title":"Life Sci."},{"key":"ref_517","doi-asserted-by":"crossref","first-page":"4255","DOI":"10.1002\/jcb.27711","article-title":"MiR-330-3p suppresses phosphoglycerate mutase family member 5 -inducted mitophagy to alleviate hepatic ischemia-reperfusion injury","volume":"120","author":"Sun","year":"2019","journal-title":"J. Cell Biochem."},{"key":"ref_518","doi-asserted-by":"crossref","first-page":"248","DOI":"10.4161\/auto.7.2.14347","article-title":"Selective taste of ethanol-induced autophagy for mitochondria and lipid droplets","volume":"7","author":"Ding","year":"2011","journal-title":"Autophagy"},{"key":"ref_519","doi-asserted-by":"crossref","first-page":"8613","DOI":"10.1016\/j.biomaterials.2011.07.047","article-title":"The association of autophagy with polyethylenimine-induced cytotoxicity in nephritic and hepatic cell lines","volume":"32","author":"Gao","year":"2011","journal-title":"Biomaterials"},{"key":"ref_520","doi-asserted-by":"crossref","first-page":"2428","DOI":"10.1172\/JCI60580","article-title":"Thyroid hormone stimulates hepatic lipid catabolism via activation of autophagy","volume":"122","author":"Sinha","year":"2012","journal-title":"J. Clin. Investig."},{"key":"ref_521","doi-asserted-by":"crossref","first-page":"20","DOI":"10.4161\/auto.26126","article-title":"Chromosome 19 open reading frame 80 is upregulated by thyroid hormone and modulates autophagy and lipid metabolism","volume":"10","author":"Tseng","year":"2014","journal-title":"Autophagy"},{"key":"ref_522","doi-asserted-by":"crossref","first-page":"896","DOI":"10.1091\/mbc.e11-09-0785","article-title":"Mammalian Atg2 proteins are essential for autophagosome formation and important for regulation of size and distribution of lipid droplets","volume":"23","author":"Velikkakath","year":"2012","journal-title":"Mol. Biol. Cell"},{"key":"ref_523","doi-asserted-by":"crossref","first-page":"1131","DOI":"10.4161\/auto.25063","article-title":"Functions of autophagy in normal and diseased liver","volume":"9","author":"Czaja","year":"2013","journal-title":"Autophagy"},{"key":"ref_524","doi-asserted-by":"crossref","first-page":"1895","DOI":"10.1053\/j.gastro.2011.04.038","article-title":"Functions of autophagy in hepatic and pancreatic physiology and disease","volume":"140","author":"Czaja","year":"2011","journal-title":"Gastroenterology"},{"key":"ref_525","doi-asserted-by":"crossref","first-page":"1123","DOI":"10.1016\/j.jhep.2010.07.006","article-title":"Autophagy in liver diseases","volume":"53","author":"Rautou","year":"2010","journal-title":"J. Hepatol."},{"key":"ref_526","doi-asserted-by":"crossref","first-page":"293","DOI":"10.1093\/ajcp\/78.3.293","article-title":"The significance of giant mitochondria in liver biopsies as observed by light microscopy","volume":"78","author":"Stewart","year":"1982","journal-title":"Am. J. Clin. Pathol."},{"key":"ref_527","doi-asserted-by":"crossref","first-page":"1383","DOI":"10.1016\/S0016-5085(19)31518-5","article-title":"Giant mitochondria in hepatocytes: A diagnostic hint for alcoholic liver disease","volume":"73","author":"Bruguera","year":"1977","journal-title":"Gastroenterology"},{"key":"ref_528","doi-asserted-by":"crossref","first-page":"8271","DOI":"10.1016\/S0021-9258(19)43224-9","article-title":"Mitochondrial functions in an ethanol-induced fatty liver","volume":"248","author":"Gordon","year":"1973","journal-title":"J. Biol. Chem."},{"key":"ref_529","doi-asserted-by":"crossref","first-page":"311","DOI":"10.1007\/s10735-013-9483-x","article-title":"Elevated autophagic sequestration of mitochondria and lipid droplets in steatotic hepatocytes of chronic ethanol-treated rats: An immunohistochemical and electron microscopic study","volume":"44","author":"Eid","year":"2013","journal-title":"J. Mol. Histol."},{"key":"ref_530","first-page":"1143","article-title":"Ethanol-induced mitophagy in liver is associated with activation of the PINK1-Parkin pathway triggered by oxidative DNA damage","volume":"31","author":"Eid","year":"2016","journal-title":"Histol. Histopathol."},{"key":"ref_531","doi-asserted-by":"crossref","unstructured":"Eid, N., Ito, Y., Horibe, A., Otsuki, Y., and Kondo, Y. (2019). Ethanol-Induced Mitochondrial Damage in Sertoli Cells is Associated with Parkin Overexpression and Activation of Mitophagy. Cells, 8.","DOI":"10.3390\/cells8030283"},{"key":"ref_532","doi-asserted-by":"crossref","unstructured":"Yu, X., Xu, Y., Zhang, S., Sun, J., Liu, P., Xiao, L., Tang, Y., Liu, L., and Yao, P. (2016). Quercetin Attenuates Chronic Ethanol-Induced Hepatic Mitochondrial Damage through Enhanced Mitophagy. Nutrients, 8.","DOI":"10.3390\/nu8010027"},{"key":"ref_533","doi-asserted-by":"crossref","first-page":"430","DOI":"10.1016\/S0168-8278(99)80033-6","article-title":"Mitochondrial abnormalities in non-alcoholic steatohepatitis","volume":"31","author":"Caldwell","year":"1999","journal-title":"J. Hepatol."},{"key":"ref_534","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1002\/hep.27420","article-title":"ALCAT1 controls mitochondrial etiology of fatty liver diseases, linking defective mitophagy to steatosis","volume":"61","author":"Wang","year":"2015","journal-title":"Hepatology"},{"key":"ref_535","doi-asserted-by":"crossref","first-page":"46","DOI":"10.1186\/s13578-016-0113-7","article-title":"Thyroid hormone-mediated autophagy and mitochondrial turnover in NAFLD","volume":"6","author":"Sinha","year":"2016","journal-title":"Cell Biosci."},{"key":"ref_536","doi-asserted-by":"crossref","first-page":"90","DOI":"10.1038\/s41419-017-0136-y","article-title":"Differential effects of reticulophagy and mitophagy on nonalcoholic fatty liver disease","volume":"9","author":"Pang","year":"2018","journal-title":"Cell Death Dis."},{"key":"ref_537","doi-asserted-by":"crossref","first-page":"588","DOI":"10.1016\/j.cmet.2018.06.014","article-title":"Mitochondrial Stasis Reveals p62-Mediated Ubiquitination in Parkin-Independent Mitophagy and Mitigates Nonalcoholic Fatty Liver Disease","volume":"28","author":"Yamada","year":"2018","journal-title":"Cell Metab."},{"key":"ref_538","doi-asserted-by":"crossref","first-page":"2371","DOI":"10.1074\/mcp.RA118.000961","article-title":"Hepatic Mitochondrial Defects in a Nonalcoholic Fatty Liver Disease Mouse Model Are Associated with Increased Degradation of Oxidative Phosphorylation Subunits","volume":"17","author":"Lee","year":"2018","journal-title":"Mol. Cell Proteom."},{"key":"ref_539","doi-asserted-by":"crossref","first-page":"749","DOI":"10.1038\/s41374-018-0177-6","article-title":"Impaired mitophagy triggers NLRP3 inflammasome activation during the progression from nonalcoholic fatty liver to nonalcoholic steatohepatitis","volume":"99","author":"Zhang","year":"2019","journal-title":"Lab. Investig."},{"key":"ref_540","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1146\/annurev-pathol-020117-043617","article-title":"Recent Insights into the Pathogenesis of Nonalcoholic Fatty Liver Disease","volume":"13","author":"Arab","year":"2018","journal-title":"Annu. Rev. Pathol."},{"key":"ref_541","doi-asserted-by":"crossref","first-page":"1864307","DOI":"10.1155\/2018\/1864307","article-title":"Exenatide Delays the Progression of Nonalcoholic Fatty Liver Disease in C57BL\/6 Mice, Which May Involve Inhibition of the NLRP3 Inflammasome through the Mitophagy Pathway","volume":"2018","author":"Shao","year":"2018","journal-title":"Gastroenterol. Res. Pract."},{"key":"ref_542","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1016\/j.redox.2018.07.011","article-title":"Therapeutic effect of Sirtuin 3 on ameliorating nonalcoholic fatty liver disease: The role of the ERK-CREB pathway and Bnip3-mediated mitophagy","volume":"18","author":"Li","year":"2018","journal-title":"Redox Biol."},{"key":"ref_543","doi-asserted-by":"crossref","first-page":"172715","DOI":"10.1016\/j.ejphar.2019.172715","article-title":"Liraglutide ameliorates non-alcoholic steatohepatitis by inhibiting NLRP3 inflammasome and pyroptosis activation via mitophagy","volume":"864","author":"Yu","year":"2019","journal-title":"Eur. J. Pharmacol."},{"key":"ref_544","doi-asserted-by":"crossref","first-page":"101120","DOI":"10.1016\/j.redox.2019.101120","article-title":"Mst1 inhibition attenuates non-alcoholic fatty liver disease via reversing Parkin-related mitophagy","volume":"21","author":"Zhou","year":"2019","journal-title":"Redox Biol."},{"key":"ref_545","first-page":"404","article-title":"Alteration of the mitochondrial pattern in the liver of tumor-bearing mice","volume":"11","author":"Annau","year":"1951","journal-title":"Cancer Res."},{"key":"ref_546","doi-asserted-by":"crossref","first-page":"355","DOI":"10.1126\/science.113.2935.355","article-title":"Proteins of liver and hepatoma mitochondria","volume":"113","author":"Hogeboom","year":"1951","journal-title":"Science"},{"key":"ref_547","doi-asserted-by":"crossref","first-page":"403","DOI":"10.1080\/15287397909529757","article-title":"Ultrastructure of hepatocellular tumors","volume":"5","author":"Hruban","year":"1979","journal-title":"J. Toxicol. Environ. Health"},{"key":"ref_548","first-page":"393","article-title":"Biology of hepatocellular neoplasia in the mouse. III. Electron microscopy of safrole-induced hepatocellular adenomas and hepatocellular carcinomas","volume":"67","author":"Lipsky","year":"1981","journal-title":"J. Natl. Cancer Inst."},{"key":"ref_549","doi-asserted-by":"crossref","first-page":"286","DOI":"10.1002\/hep.21509","article-title":"Concanavalin A induces autophagy in hepatoma cells and has a therapeutic effect in a murine in situ hepatoma model","volume":"45","author":"Chang","year":"2007","journal-title":"Hepatology"},{"key":"ref_550","doi-asserted-by":"crossref","first-page":"402","DOI":"10.4161\/auto.4280","article-title":"Induction of autophagy by concanavalin A and its application in anti-tumor therapy","volume":"3","author":"Lei","year":"2007","journal-title":"Autophagy"},{"key":"ref_551","doi-asserted-by":"crossref","first-page":"779","DOI":"10.1097\/CAD.0b013e32832f4e6f","article-title":"Alterations of cellular organelles in human liver-derived hepatoma G2 cells induced by adriamycin","volume":"20","author":"Qian","year":"2009","journal-title":"Anticancer Drugs"},{"key":"ref_552","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1016\/j.ejps.2011.04.002","article-title":"Curcumin enhanced adriamycin-induced human liver-derived Hepatoma G2 cell death through activation of mitochondria-mediated apoptosis and autophagy","volume":"43","author":"Qian","year":"2011","journal-title":"Eur J. Pharm. Sci."},{"key":"ref_553","doi-asserted-by":"crossref","first-page":"396","DOI":"10.1111\/jpi.12358","article-title":"Melatonin-induced increase in sensitivity of human hepatocellular carcinoma cells to sorafenib is associated with reactive oxygen species production and mitophagy","volume":"61","author":"Ordonez","year":"2016","journal-title":"J. Pineal Res."},{"key":"ref_554","doi-asserted-by":"crossref","unstructured":"Liu, K., Shi, Y., Guo, X.H., Ouyang, Y.B., Wang, S.S., Liu, D.J., Wang, A.N., Li, N., and Chen, D.X. (2014). Phosphorylated AKT inhibits the apoptosis induced by DRAM-mediated mitophagy in hepatocellular carcinoma by preventing the translocation of DRAM to mitochondria. Cell Death Dis., 5.","DOI":"10.1038\/cddis.2014.51"},{"key":"ref_555","doi-asserted-by":"crossref","first-page":"604","DOI":"10.1002\/hep.30191","article-title":"FUN14 Domain-Containing 1-Mediated Mitophagy Suppresses Hepatocarcinogenesis by Inhibition of Inflammasome Activation in Mice","volume":"69","author":"Li","year":"2019","journal-title":"Hepatology"},{"key":"ref_556","doi-asserted-by":"crossref","first-page":"999","DOI":"10.1080\/15548627.2016.1166318","article-title":"Increased mitochondrial fission promotes autophagy and hepatocellular carcinoma cell survival through the ROS-modulated coordinated regulation of the NFKB and TP53 pathways","volume":"12","author":"Huang","year":"2016","journal-title":"Autophagy"},{"key":"ref_557","doi-asserted-by":"crossref","first-page":"281","DOI":"10.1016\/j.molcel.2017.09.022","article-title":"Mitophagy Controls the Activities of Tumor Suppressor p53 to Regulate Hepatic Cancer Stem Cells","volume":"68","author":"Liu","year":"2017","journal-title":"Mol. Cell"},{"key":"ref_558","doi-asserted-by":"crossref","first-page":"68","DOI":"10.1016\/j.yexcr.2015.04.016","article-title":"ABT737 enhances cholangiocarcinoma sensitivity to cisplatin through regulation of mitochondrial dynamics","volume":"335","author":"Fan","year":"2015","journal-title":"Exp. Cell Res."},{"key":"ref_559","doi-asserted-by":"crossref","first-page":"18036","DOI":"10.1074\/jbc.M111.320085","article-title":"Replication of hepatitis C virus RNA on autophagosomal membranes","volume":"287","author":"Sir","year":"2012","journal-title":"J. Biol. Chem."},{"key":"ref_560","doi-asserted-by":"crossref","first-page":"2230","DOI":"10.1099\/vir.0.022186-0","article-title":"Ultrastructural and biochemical analyses of hepatitis C virus-associated host cell membranes","volume":"91","author":"Ferraris","year":"2010","journal-title":"J. Gen. Virol."},{"key":"ref_561","doi-asserted-by":"crossref","unstructured":"Kim, J.Y., Wang, L., Lee, J., and Ou, J.J. (2017). Hepatitis C Virus Induces the Localization of Lipid Rafts to Autophagosomes for Its RNA Replication. J. Virol., 91.","DOI":"10.1128\/JVI.00541-17"},{"key":"ref_562","doi-asserted-by":"crossref","first-page":"406","DOI":"10.1002\/hep.24073","article-title":"Knockdown of autophagy enhances the innate immune response in hepatitis C virus-infected hepatocytes","volume":"53","author":"Shrivastava","year":"2011","journal-title":"Hepatology"},{"key":"ref_563","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.virol.2010.05.032","article-title":"Autophagy protein ATG5 interacts transiently with the hepatitis C virus RNA polymerase (NS5B) early during infection","volume":"405","author":"Guevin","year":"2010","journal-title":"Virology"},{"key":"ref_564","doi-asserted-by":"crossref","unstructured":"Wang, L., Kim, J.Y., Liu, H.M., Lai, M.M.C., and Ou, J.J. (2017). HCV-induced autophagosomes are generated via homotypic fusion of phagophores that mediate HCV RNA replication. PLoS Pathog., 13.","DOI":"10.1371\/journal.ppat.1006609"},{"key":"ref_565","doi-asserted-by":"crossref","first-page":"937","DOI":"10.4161\/auto.5.7.9243","article-title":"Knockdown of autophagy-related gene decreases the production of infectious hepatitis C virus particles","volume":"5","author":"Tanida","year":"2009","journal-title":"Autophagy"},{"key":"ref_566","doi-asserted-by":"crossref","first-page":"1387","DOI":"10.1128\/JVI.02383-15","article-title":"Knockdown of Autophagy Inhibits Infectious Hepatitis C Virus Release by the Exosomal Pathway","volume":"90","author":"Shrivastava","year":"2016","journal-title":"J. Virol."},{"key":"ref_567","doi-asserted-by":"crossref","unstructured":"Kim, J.Y., and Ou, J.J. (2018). Regulation of Apolipoprotein E Trafficking by Hepatitis C Virus-induced Autophagy. J. Virol.","DOI":"10.1128\/JVI.00211-18"},{"key":"ref_568","doi-asserted-by":"crossref","first-page":"5989","DOI":"10.1128\/JVI.00551-16","article-title":"The Autophagosomal SNARE Protein Syntaxin 17 Is an Essential Factor for the Hepatitis C Virus Life Cycle","volume":"90","author":"Ren","year":"2016","journal-title":"J. Virol."},{"key":"ref_569","doi-asserted-by":"crossref","first-page":"1150","DOI":"10.1016\/j.jhep.2011.04.025","article-title":"Activation of unfolded protein response and autophagy during HCV infection modulates innate immune response","volume":"55","author":"Estrabaud","year":"2011","journal-title":"J. Hepatol."},{"key":"ref_570","doi-asserted-by":"crossref","first-page":"13185","DOI":"10.1128\/JVI.06099-11","article-title":"Dysfunction of autophagy participates in vacuole formation and cell death in cells replicating hepatitis C virus","volume":"85","author":"Taguwa","year":"2011","journal-title":"J. Virol."},{"key":"ref_571","doi-asserted-by":"crossref","first-page":"644","DOI":"10.1053\/j.gastro.2011.11.033","article-title":"Autophagy protects cells from HCV-induced defects in lipid metabolism","volume":"142","author":"Vescovo","year":"2012","journal-title":"Gastroenterology"},{"key":"ref_572","doi-asserted-by":"crossref","unstructured":"Kim, S.J., Syed, G.H., and Siddiqui, A. (2013). Hepatitis C virus induces the mitochondrial translocation of Parkin and subsequent mitophagy. PLoS Pathog., 9.","DOI":"10.1371\/journal.ppat.1003285"},{"key":"ref_573","doi-asserted-by":"crossref","unstructured":"Chu, V.C., Bhattacharya, S., Nomoto, A., Lin, J., Zaidi, S.K., Oberley, T.D., Weinman, S.A., Azhar, S., and Huang, T.T. (2011). Persistent expression of hepatitis C virus non-structural proteins leads to increased autophagy and mitochondrial injury in human hepatoma cells. PLoS ONE, 6.","DOI":"10.1371\/journal.pone.0028551"},{"key":"ref_574","doi-asserted-by":"crossref","first-page":"6413","DOI":"10.1073\/pnas.1321114111","article-title":"Hepatitis C virus triggers mitochondrial fission and attenuates apoptosis to promote viral persistence","volume":"111","author":"Kim","year":"2014","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_575","doi-asserted-by":"crossref","unstructured":"Jassey, A., Liu, C.H., Changou, C.A., Richardson, C.D., Hsu, H.Y., and Lin, L.T. (2019). Hepatitis C Virus Non-Structural Protein 5A (NS5A) Disrupts Mitochondrial Dynamics and Induces Mitophagy. Cells, 8.","DOI":"10.3390\/cells8040290"},{"key":"ref_576","doi-asserted-by":"crossref","first-page":"3026","DOI":"10.1016\/j.ajpath.2014.07.024","article-title":"Hepatitis C virus core protein suppresses mitophagy by interacting with parkin in the context of mitochondrial depolarization","volume":"184","author":"Hara","year":"2014","journal-title":"Am. J. Pathol."},{"key":"ref_577","doi-asserted-by":"crossref","unstructured":"Kim, S.J., Khan, M., Quan, J., Till, A., Subramani, S., and Siddiqui, A. (2013). Hepatitis B virus disrupts mitochondrial dynamics: Induces fission and mitophagy to attenuate apoptosis. PLoS Pathog., 9.","DOI":"10.1371\/journal.ppat.1003722"},{"key":"ref_578","doi-asserted-by":"crossref","first-page":"1809","DOI":"10.1172\/JCI20039","article-title":"Promotion of tumorigenesis by heterozygous disruption of the beclin 1 autophagy gene","volume":"112","author":"Qu","year":"2003","journal-title":"J. Clin. Investig."},{"key":"ref_579","doi-asserted-by":"crossref","first-page":"60","DOI":"10.1002\/hep.22581","article-title":"Hepatitis B virus X protein sensitizes cells to starvation-induced autophagy via up-regulation of beclin 1 expression","volume":"49","author":"Tang","year":"2009","journal-title":"Hepatology"},{"key":"ref_580","doi-asserted-by":"crossref","first-page":"6319","DOI":"10.1128\/JVI.02627-10","article-title":"Subversion of cellular autophagy machinery by hepatitis B virus for viral envelopment","volume":"85","author":"Li","year":"2011","journal-title":"J. Virol."},{"key":"ref_581","doi-asserted-by":"crossref","first-page":"974","DOI":"10.1002\/hep.30248","article-title":"Hepatitis B Virus Induces Autophagy to Promote its Replication by the Axis of miR-192-3p-XIAP Through NF kappa B Signaling","volume":"69","author":"Wang","year":"2019","journal-title":"Hepatology"},{"key":"ref_582","doi-asserted-by":"crossref","unstructured":"Chen, L., Ming, X., Li, W., Bi, M., Yan, B., Wang, X., Yang, P., and Yang, B. (2020). The microRNA-155 mediates hepatitis B virus replication by reinforcing SOCS1 signalling-induced autophagy. Cell Biochem. Funct.","DOI":"10.1002\/cbf.3488"},{"key":"ref_583","first-page":"1696","article-title":"HBV secretion is regulated through the activation of endocytic and autophagic compartments mediated by Rab7 stimulation","volume":"128","author":"Inoue","year":"2015","journal-title":"J. Cell Sci."},{"key":"ref_584","doi-asserted-by":"crossref","unstructured":"Doring, T., Zeyen, L., Bartusch, C., and Prange, R. (2018). Hepatitis B Virus Subverts the Autophagy Elongation Complex Atg5-12\/16L1 and Does Not Require Atg8\/LC3 Lipidation for Viral Maturation. J. Virol., 92.","DOI":"10.1128\/JVI.01513-17"},{"key":"ref_585","doi-asserted-by":"crossref","first-page":"2382","DOI":"10.1002\/jcp.24967","article-title":"Autophagy Mediates HBx-Induced Nuclear Factor-kappaB Activation and Release of IL-6, IL-8, and CXCL2 in Hepatocytes","volume":"230","author":"Luo","year":"2015","journal-title":"J. Cell Physiol."},{"key":"ref_586","doi-asserted-by":"crossref","first-page":"805","DOI":"10.4049\/jimmunol.1800871","article-title":"Hepatitis B Virus Inhibits Neutrophil Extracellular Trap Release by Modulating Reactive Oxygen Species Production and Autophagy","volume":"202","author":"Hu","year":"2019","journal-title":"J. Immunol."},{"key":"ref_587","doi-asserted-by":"crossref","first-page":"505","DOI":"10.1002\/hep.26659","article-title":"Autophagy suppresses tumorigenesis of hepatitis B virus-associated hepatocellular carcinoma through degradation of microRNA-224","volume":"59","author":"Lan","year":"2014","journal-title":"Hepatology"},{"key":"ref_588","doi-asserted-by":"crossref","first-page":"6023","DOI":"10.1096\/fj.201801995RR","article-title":"Synaptosomal-associated protein 29 is required for the autophagic degradation of hepatitis B virus","volume":"33","author":"Lin","year":"2019","journal-title":"FASEB J."},{"key":"ref_589","doi-asserted-by":"crossref","first-page":"548","DOI":"10.1080\/15548627.2019.1632104","article-title":"Glucosamine promotes hepatitis B virus replication through its dual effects in suppressing autophagic degradation and inhibiting MTORC1 signaling","volume":"16","author":"Lin","year":"2020","journal-title":"Autophagy"},{"key":"ref_590","doi-asserted-by":"crossref","first-page":"416","DOI":"10.4161\/auto.27286","article-title":"Hepatitis B virus X protein inhibits autophagic degradation by impairing lysosomal maturation","volume":"10","author":"Liu","year":"2014","journal-title":"Autophagy"},{"key":"ref_591","doi-asserted-by":"crossref","first-page":"5274","DOI":"10.1038\/onc.2017.136","article-title":"Thyroid hormone protects hepatocytes from HBx-induced carcinogenesis by enhancing mitochondrial turnover","volume":"36","author":"Chi","year":"2017","journal-title":"Oncogene"},{"key":"ref_592","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1016\/j.yexcr.2018.04.016","article-title":"Hepatitis B Virus X protein elevates Parkin-mediated mitophagy through Lon Peptidase in starvation","volume":"368","author":"Huang","year":"2018","journal-title":"Exp. Cell Res."},{"key":"ref_593","doi-asserted-by":"crossref","first-page":"383","DOI":"10.1111\/jpi.12319","article-title":"Melatonin enhances mitophagy and mitochondrial biogenesis in rats with carbon tetrachloride-induced liver fibrosis","volume":"60","author":"Kang","year":"2016","journal-title":"J. Pineal Res."},{"key":"ref_594","doi-asserted-by":"crossref","first-page":"e12731","DOI":"10.1111\/cpr.12731","article-title":"TIM-4 interference in Kupffer cells against CCL4-induced liver fibrosis by mediating Akt1\/Mitophagy signalling pathway","volume":"53","author":"Wu","year":"2020","journal-title":"Cell Prolif."},{"key":"ref_595","doi-asserted-by":"crossref","first-page":"178","DOI":"10.1016\/j.ecoenv.2018.08.050","article-title":"PM2.5 induces liver fibrosis via triggering ROS-mediated mitophagy","volume":"167","author":"Qiu","year":"2019","journal-title":"Ecotoxicol. Environ. Saf."},{"key":"ref_596","doi-asserted-by":"crossref","first-page":"G374","DOI":"10.1152\/ajpgi.00032.2018","article-title":"Role of mitophagy regulation by ROS in hepatic stellate cells during acute liver failure","volume":"315","author":"Tian","year":"2018","journal-title":"Am. J. Physiol. Gastrointest. Liver Physiol."},{"key":"ref_597","doi-asserted-by":"crossref","first-page":"56","DOI":"10.1038\/s41392-019-0094-1","article-title":"DNA-PKcs promotes alcohol-related liver disease by activating Drp1-related mitochondrial fission and repressing FUNDC1-required mitophagy","volume":"4","author":"Zhou","year":"2019","journal-title":"Signal. Transduct. Target. Ther."},{"key":"ref_598","doi-asserted-by":"crossref","first-page":"eaam5855","DOI":"10.1126\/scisignal.aam5855","article-title":"Thyroid hormone receptor and ERRalpha coordinately regulate mitochondrial fission, mitophagy, biogenesis, and function","volume":"11","author":"Singh","year":"2018","journal-title":"Sci. Signal."},{"key":"ref_599","doi-asserted-by":"crossref","unstructured":"Dumas, K., Ayachi, C., Gilleron, J., Lacas-Gervais, S., Pastor, F., Favier, F.B., Peraldi, P., Vaillant, N., Yvan-Charvet, L., and Bonnafous, S. (2020). REDD1 deficiency protects against nonalcoholic hepatic steatosis induced by high-fat diet. FASEB J.","DOI":"10.1096\/fj.201901799RR"},{"key":"ref_600","doi-asserted-by":"crossref","first-page":"31484","DOI":"10.1074\/jbc.M109.033936","article-title":"Hepatic autophagy is suppressed in the presence of insulin resistance and hyperinsulinemia: Inhibition of FoxO1-dependent expression of key autophagy genes by insulin","volume":"284","author":"Liu","year":"2009","journal-title":"J. Biol. Chem."},{"key":"ref_601","doi-asserted-by":"crossref","first-page":"E105","DOI":"10.1152\/ajpendo.00042.2016","article-title":"Reduced intestinal lipid absorption and body weight-independent improvements in insulin sensitivity in high-fat diet-fed Park2 knockout mice","volume":"311","author":"Costa","year":"2016","journal-title":"Am. J. Physiol. Endocrinol. Metab."},{"key":"ref_602","doi-asserted-by":"crossref","first-page":"e14281","DOI":"10.14814\/phy2.14281","article-title":"Hepatic insulin sensitivity is improved in high-fat diet-fed Park2 knockout mice in association with increased hepatic AMPK activation and reduced steatosis","volume":"7","author":"Edmunds","year":"2019","journal-title":"Physiol. Rep."},{"key":"ref_603","doi-asserted-by":"crossref","first-page":"1882","DOI":"10.1080\/15548627.2019.1596482","article-title":"Deficiency of mitophagy receptor FUNDC1 impairs mitochondrial quality and aggravates dietary-induced obesity and metabolic syndrome","volume":"15","author":"Wu","year":"2019","journal-title":"Autophagy"},{"key":"ref_604","doi-asserted-by":"crossref","first-page":"1585","DOI":"10.1016\/j.chembiol.2014.09.019","article-title":"PMI: A DeltaPsim independent pharmacological regulator of mitophagy","volume":"21","author":"East","year":"2014","journal-title":"Chem. Biol."},{"key":"ref_605","doi-asserted-by":"crossref","first-page":"879","DOI":"10.1038\/nm.4132","article-title":"Urolithin A induces mitophagy and prolongs lifespan in C. elegans and increases muscle function in rodents","volume":"22","author":"Ryu","year":"2016","journal-title":"Nat. Med."},{"key":"ref_606","doi-asserted-by":"crossref","first-page":"299","DOI":"10.1016\/j.cell.2019.02.013","article-title":"Mitochondrial Permeability Uncouples Elevated Autophagy and Lifespan Extension","volume":"177","author":"Zhou","year":"2019","journal-title":"Cell"}],"container-title":["Cells"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2073-4409\/9\/4\/831\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T09:13:31Z","timestamp":1760174011000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2073-4409\/9\/4\/831"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,3,30]]},"references-count":606,"journal-issue":{"issue":"4","published-online":{"date-parts":[[2020,4]]}},"alternative-id":["cells9040831"],"URL":"https:\/\/doi.org\/10.3390\/cells9040831","relation":{},"ISSN":["2073-4409"],"issn-type":[{"value":"2073-4409","type":"electronic"}],"subject":[],"published":{"date-parts":[[2020,3,30]]}}}