{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,22]],"date-time":"2026-10-22T10:05:19Z","timestamp":1792663519300,"version":"4.5.0"},"reference-count":179,"publisher":"MDPI AG","issue":"17","license":[{"start":{"date-parts":[[2019,9,3]],"date-time":"2019-09-03T00:00:00Z","timestamp":1567468800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["RE 1575\/2-1"],"award-info":[{"award-number":["RE 1575\/2-1"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100009400","name":"Medizinische Fakult\u00e4t, Heinrich-Heine-Universit\u00e4t D\u00fcsseldorf","doi-asserted-by":"publisher","award":["Foko 37\/2015"],"award-info":[{"award-number":["Foko 37\/2015"]}],"id":[{"id":"10.13039\/501100009400","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Mitochondria are vital cellular organelles involved in a plethora of cellular processes such as energy conversion, calcium homeostasis, heme biogenesis, regulation of apoptosis and ROS reactive oxygen species (ROS) production. Although they are frequently depicted as static bean-shaped structures, our view has markedly changed over the past few decades as many studies have revealed a remarkable dynamicity of mitochondrial shapes and sizes both at the cellular and intra-mitochondrial levels. Aberrant changes in mitochondrial dynamics and cristae structure are associated with ageing and numerous human diseases (e.g., cancer, diabetes, various neurodegenerative diseases, types of neuro- and myopathies). Another unique feature of mitochondria is that they harbor their own genome, the mitochondrial DNA (mtDNA). MtDNA exists in several hundreds to thousands of copies per cell and is arranged and packaged in the mitochondrial matrix in structures termed mt-nucleoids. Many human diseases are mechanistically linked to mitochondrial dysfunction and alteration of the number and\/or the integrity of mtDNA. In particular, several recent studies identified remarkable and partly unexpected links between mitochondrial structure, fusion and fission dynamics, and mtDNA. In this review, we will provide an overview about these recent insights and aim to clarify how mitochondrial dynamics, cristae ultrastructure and mtDNA structure influence each other and determine mitochondrial functions.<\/jats:p>","DOI":"10.3390\/ijms20174311","type":"journal-article","created":{"date-parts":[[2019,9,4]],"date-time":"2019-09-04T08:28:13Z","timestamp":1567585693000},"page":"4311","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":88,"title":["Functional Interplay between Cristae Biogenesis, Mitochondrial Dynamics and Mitochondrial DNA Integrity"],"prefix":"10.3390","volume":"20","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-5888-7834","authenticated-orcid":false,"given":"Arun Kumar","family":"Kondadi","sequence":"first","affiliation":[{"name":"Institute of Biochemistry and Molecular Biology I, Medical Faculty, Heinrich Heine University D\u00fcsseldorf, 40225 D\u00fcsseldorf, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7337-6007","authenticated-orcid":false,"given":"Ruchika","family":"Anand","sequence":"additional","affiliation":[{"name":"Institute of Biochemistry and Molecular Biology I, Medical Faculty, Heinrich Heine University D\u00fcsseldorf, 40225 D\u00fcsseldorf, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9340-3113","authenticated-orcid":false,"given":"Andreas S.","family":"Reichert","sequence":"additional","affiliation":[{"name":"Institute of Biochemistry and Molecular Biology I, Medical Faculty, Heinrich Heine University D\u00fcsseldorf, 40225 D\u00fcsseldorf, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2019,9,3]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"260","DOI":"10.1006\/jsbi.1997.3885","article-title":"Electron tomography of neuronal mitochondria: Three-dimensional structure and organization of cristae and membrane contacts","volume":"119","author":"Perkins","year":"1997","journal-title":"J. Struct. Biol."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"431","DOI":"10.1023\/A:1020586012561","article-title":"Electron tomography of mitochondria from brown adipocytes reveals crista junctions","volume":"30","author":"Perkins","year":"1998","journal-title":"J. Bioenerg. Biomembr."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1016\/j.bbamcr.2008.06.013","article-title":"Cristae formation-linking ultrastructure and function of mitochondria","volume":"1793","author":"Zick","year":"2009","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1083\/jcb.200605138","article-title":"Dynamic subcompartmentalization of the mitochondrial inner membrane","volume":"175","author":"Vogel","year":"2006","journal-title":"J. Cell Biol."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1016\/S0968-0004(96)30050-9","article-title":"Reconsidering mitochondrial structure: New views of an old organelle","volume":"22","author":"Mannella","year":"1997","journal-title":"Trends Biochem. Sci."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1083\/jcb.30.2.269","article-title":"Ultrastructural bases for metabolically linked mechanical activity in mitochondria. I. Reversible ultrastructural changes with change in metabolic steady state in isolated liver mitochondria","volume":"30","author":"Hackenbrock","year":"1966","journal-title":"J. Cell Biol."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"598","DOI":"10.1073\/pnas.61.2.598","article-title":"Chemical and physical fixation of isolated mitochondria in low-energy and high-energy states","volume":"61","author":"Hackenbrock","year":"1968","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1016\/S1534-5807(01)00116-2","article-title":"A distinct pathway remodels mitochondrial cristae and mobilizes cytochrome c during apoptosis","volume":"2","author":"Scorrano","year":"2002","journal-title":"Dev. Cell"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1038\/79944","article-title":"OPA1, encoding a dynamin-related GTPase, is mutated in autosomal dominant optic atrophy linked to chromosome 3q28","volume":"26","author":"Alexander","year":"2000","journal-title":"Nat. Genet."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"1893","DOI":"10.1093\/hmg\/ddr071","article-title":"A clinically complex form of dominant optic atrophy (OPA8) maps on chromosome 16","volume":"20","author":"Carelli","year":"2011","journal-title":"Hum. Mol. Genet."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1038\/79936","article-title":"Nuclear gene OPA1, encoding a mitochondrial dynamin-related protein, is mutated in dominant optic atrophy","volume":"26","author":"Delettre","year":"2000","journal-title":"Nat. Genet."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1136\/jmedgenet-2015-103361","article-title":"Fatal infantile mitochondrial encephalomyopathy, hypertrophic cardiomyopathy and optic atrophy associated with a homozygous OPA1 mutation","volume":"53","author":"Spiegel","year":"2016","journal-title":"J. Med. Genet."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1016\/j.bbamcr.2012.06.025","article-title":"Proteolytic control of mitochondrial function and morphogenesis","volume":"1833","author":"Anand","year":"2013","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"2297","DOI":"10.1242\/jcs.159186","article-title":"OPA1 processing in cell death and disease-the long and short of it","volume":"129","author":"MacVicar","year":"2016","journal-title":"J. Cell Sci."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"919","DOI":"10.1083\/jcb.201308006","article-title":"The i-AAA protease YME1L and OMA1 cleave OPA1 to balance mitochondrial fusion and fission","volume":"204","author":"Anand","year":"2014","journal-title":"J. Cell Biol."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1016\/j.cell.2006.06.025","article-title":"OPA1 controls apoptotic cristae remodeling independently from mitochondrial fusion","volume":"126","author":"Frezza","year":"2006","journal-title":"Cell"},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"7743","DOI":"10.1074\/jbc.C200677200","article-title":"Loss of OPA1 perturbates the mitochondrial inner membrane structure and integrity, leading to cytochrome c release and apoptosis","volume":"278","author":"Olichon","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"2557","DOI":"10.1016\/j.celrep.2017.05.073","article-title":"OPA1 Isoforms in the Hierarchical Organization of Mitochondrial Functions","volume":"19","author":"Mishra","year":"2017","journal-title":"Cell Rep."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"7115","DOI":"10.1074\/jbc.M116.762567","article-title":"The short variant of the mitochondrial dynamin OPA1 maintains mitochondrial energetics and cristae structure","volume":"292","author":"Lee","year":"2017","journal-title":"J. Biol. Chem."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"e18853","DOI":"10.7554\/eLife.18853","article-title":"An evidence based hypothesis on the existence of two pathways of mitochondrial crista formation","volume":"5","author":"Harner","year":"2016","journal-title":"eLife"},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"48484","DOI":"10.1074\/jbc.M209382200","article-title":"Su e of the yeast F1Fo-ATP synthase forms homodimers","volume":"277","author":"Brunner","year":"2002","journal-title":"J. Biol. Chem."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1093\/emboj\/21.3.221","article-title":"The ATP synthase is involved in generating mitochondrial cristae morphology","volume":"21","author":"Paumard","year":"2002","journal-title":"Embo J."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"10739","DOI":"10.1074\/jbc.M111882200","article-title":"In the absence of the first membrane-spanning segment of subunit 4(b), the yeast ATP synthase is functional but does not dimerize or oligomerize","volume":"277","author":"Soubannier","year":"2002","journal-title":"J. Biol. Chem."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"4250","DOI":"10.1073\/pnas.1816556116","article-title":"Dimers of mitochondrial ATP synthase induce membrane curvature and self-assemble into rows","volume":"116","author":"Blum","year":"2019","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"1215","DOI":"10.1074\/mcp.M700076-MCP200","article-title":"High resolution clear native electrophoresis for in-gel functional assays and fluorescence studies of membrane protein complexes","volume":"6","author":"Wittig","year":"2007","journal-title":"Mol. Cell. Proteom."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"1154","DOI":"10.1038\/emboj.2008.35","article-title":"Dimer ribbons of ATP synthase shape the inner mitochondrial membrane","volume":"27","author":"Strauss","year":"2008","journal-title":"Embo J."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"14121","DOI":"10.1073\/pnas.1103621108","article-title":"Macromolecular organization of ATP synthase and complex I in whole mitochondria","volume":"108","author":"Davies","year":"2011","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"445","DOI":"10.1016\/j.molcel.2016.05.037","article-title":"Structure of a Complete ATP Synthase Dimer Reveals the Molecular Basis of Inner Mitochondrial Membrane Morphology","volume":"63","author":"Hahn","year":"2016","journal-title":"Mol. Cell"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"1047","DOI":"10.1083\/jcb.200811099","article-title":"Formation of cristae and crista junctions in mitochondria depends on antagonism between Fcj1 and Su e\/g","volume":"185","author":"Rabl","year":"2009","journal-title":"J. Cell Biol."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"694","DOI":"10.1016\/j.devcel.2011.08.026","article-title":"Dual role of mitofilin in mitochondrial membrane organization and protein biogenesis","volume":"21","author":"Muller","year":"2011","journal-title":"Dev. Cell"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"4356","DOI":"10.1038\/emboj.2011.379","article-title":"The mitochondrial contact site complex, a determinant of mitochondrial architecture","volume":"30","author":"Harner","year":"2011","journal-title":"Embo J."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"323","DOI":"10.1083\/jcb.201107053","article-title":"A mitochondrial-focused genetic interaction map reveals a scaffold-like complex required for inner membrane organization in mitochondria","volume":"195","author":"Hoppins","year":"2011","journal-title":"J. Cell Biol."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1016\/j.bbamcr.2015.10.009","article-title":"Evolution and structural organization of the mitochondrial contact site (MICOS) complex and the mitochondrial intermembrane space bridging (MIB) complex","volume":"1863","author":"Huynen","year":"2016","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"1489","DOI":"10.1016\/j.cub.2015.04.006","article-title":"Ancient homology of the mitochondrial contact site and cristae organizing system points to an endosymbiotic origin of mitochondrial cristae","volume":"25","author":"Slamovits","year":"2015","journal-title":"Curr. Biol."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"1083","DOI":"10.1083\/jcb.201401006","article-title":"Uniform nomenclature for the mitochondrial contact site and cristae organizing system","volume":"204","author":"Pfanner","year":"2014","journal-title":"J. Cell Biol."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"1481","DOI":"10.1016\/j.bbamcr.2017.05.004","article-title":"Mitochondrial Contact Site and Cristae Organizing System: A Central Player in Membrane Shaping and Crosstalk","volume":"1864","author":"Wollweber","year":"2017","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1016\/j.ceb.2016.03.013","article-title":"Mitochondrial contact site and cristae organizing system","volume":"41","author":"Horvath","year":"2016","journal-title":"Curr. Opin. Cell Biol."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"3545","DOI":"10.1016\/j.febslet.2007.06.052","article-title":"The mitochondrial inner membrane protein mitofilin exists as a complex with SAM50, metaxins 1 and 2, coiled-coil-helix coiled-coil-helix domain-containing protein 3 and 6 and DnaJC11","volume":"581","author":"Xie","year":"2007","journal-title":"FEBS Lett."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"2143","DOI":"10.1091\/mbc.e11-10-0831","article-title":"The C-terminal domain of Fcj1 is required for formation of crista junctions and interacts with the TOB\/SAM complex in mitochondria","volume":"23","author":"Barrera","year":"2012","journal-title":"Mol. Biol. Cell"},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"1173","DOI":"10.1128\/MCB.06388-11","article-title":"Sam50 functions in mitochondrial intermembrane space bridging and biogenesis of respiratory complexes","volume":"32","author":"Ott","year":"2012","journal-title":"Mol. Cell. Biol."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"926","DOI":"10.1038\/ng.3354","article-title":"Mutations in SLC25A46, encoding a UGO1-like protein, cause an optic atrophy spectrum disorder","volume":"47","author":"Abrams","year":"2015","journal-title":"Nat. Genet."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"3024","DOI":"10.1016\/j.celrep.2016.11.049","article-title":"Optic Atrophy 1 Is Epistatic to the Core MICOS Component MIC60 in Mitochondrial Cristae Shape Control","volume":"17","author":"Glytsou","year":"2016","journal-title":"Cell Rep."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"4157","DOI":"10.1093\/hmg\/ddw250","article-title":"Disrupted in schizophrenia 1 (DISC1) is a constituent of the mammalian mitochondrial contact site and cristae organizing system (MICOS) complex, and is essential for oxidative phosphorylation","volume":"25","author":"Llado","year":"2016","journal-title":"Hum. Mol. Genet."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"58","DOI":"10.15252\/emmm.201505496","article-title":"CHCHD10 mutations promote loss of mitochondrial cristae junctions with impaired mitochondrial genome maintenance and inhibition of apoptosis","volume":"8","author":"Genin","year":"2015","journal-title":"Embo Mol. Med."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"756","DOI":"10.1016\/j.cmet.2015.04.006","article-title":"Mic10 oligomerizes to bend mitochondrial inner membranes at cristae junctions","volume":"21","author":"Barbot","year":"2015","journal-title":"Cell Metab."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"747","DOI":"10.1016\/j.cmet.2015.04.007","article-title":"Central role of Mic10 in the mitochondrial contact site and cristae organizing system","volume":"21","author":"Bohnert","year":"2015","journal-title":"Cell Metab."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"660","DOI":"10.1016\/j.cmet.2015.04.020","article-title":"Mic10 Oligomerization Pinches off Mitochondrial Cristae","volume":"21","author":"Milenkovic","year":"2015","journal-title":"Cell Metab."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"15258","DOI":"10.1038\/ncomms15258","article-title":"Regulated membrane remodeling by Mic60 controls formation of mitochondrial crista junctions","volume":"8","author":"Hessenberger","year":"2017","journal-title":"Nat. Commun."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"889","DOI":"10.1083\/jcb.201609046","article-title":"The MICOS component Mic60 displays a conserved membrane-bending activity that is necessary for normal cristae morphology","volume":"216","author":"Tarasenko","year":"2017","journal-title":"J. Cell Biol."},{"key":"ref_50","doi-asserted-by":"crossref","unstructured":"Anand, R., Strecker, V., Urbach, J., Wittig, I., and Reichert, A.S. (2016). Mic13 Is Essential for Formation of Crista Junctions in Mammalian Cells. PLoS ONE, 11.","DOI":"10.1371\/journal.pone.0160258"},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"e06265","DOI":"10.7554\/eLife.06265","article-title":"QIL1 is a novel mitochondrial protein required for MICOS complex stability and cristae morphology","volume":"4","author":"Guarani","year":"2015","journal-title":"eLife"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"1551","DOI":"10.1016\/j.bbamcr.2015.03.004","article-title":"The non-glycosylated isoform of MIC26 is a constituent of the mammalian MICOS complex and promotes formation of crista junctions","volume":"1853","author":"Koob","year":"2015","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_53","doi-asserted-by":"crossref","unstructured":"Weber, T.A., Koob, S., Heide, H., Wittig, I., Head, B., van der Bliek, A., Brandt, U., Mittelbronn, M., and Reichert, A.S. (2013). APOOL is a cardiolipin-binding constituent of the Mitofilin\/MINOS protein complex determining cristae morphology in mammalian mitochondria. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0063683"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1515\/hsz-2013-0274","article-title":"Novel intracellular functions of apolipoproteins: The ApoO protein family as constituents of the Mitofilin\/MINOS complex determines cristae morphology in mitochondria","volume":"395","author":"Koob","year":"2014","journal-title":"Biol. Chem."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"1247","DOI":"10.1515\/hsz-2012-0239","article-title":"Mitofilin complexes: Conserved organizers of mitochondrial membrane architecture","volume":"393","author":"Zerbes","year":"2012","journal-title":"Biol. Chem."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"1066","DOI":"10.1002\/hep.30627","article-title":"Expanding and Underscoring the Hepato-Encephalopathic Phenotype of QIL1\/MIC13","volume":"70","author":"Russell","year":"2019","journal-title":"Hepatol. (Baltim. Md.)"},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"707","DOI":"10.1038\/s10038-018-0442-y","article-title":"QIL1-dependent assembly of MICOS complex-lethal mutation in C19ORF70 resulting in liver disease and severe neurological retardation","volume":"63","author":"Godiker","year":"2018","journal-title":"J. Hum. Genet."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"1778","DOI":"10.1038\/ejhg.2016.83","article-title":"Mitochondrial hepato-encephalopathy due to deficiency of QIL1\/MIC13 (C19orf70), a MICOS complex subunit","volume":"24","author":"Zeharia","year":"2016","journal-title":"Eur. J. Hum. Genet."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"e17163","DOI":"10.7554\/eLife.17163","article-title":"QIL1 mutation causes MICOS disassembly and early onset fatal mitochondrial encephalopathy with liver disease","volume":"5","author":"Guarani","year":"2016","journal-title":"eLife"},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"744","DOI":"10.1016\/j.molcel.2018.01.026","article-title":"PINK1 Phosphorylates MIC60\/Mitofilin to Control Structural Plasticity of Mitochondrial Crista Junctions","volume":"69","author":"Tsai","year":"2018","journal-title":"Mol. Cell"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"259","DOI":"10.15698\/mic2017.08.585","article-title":"Cristae architecture is determined by an interplay of the MICOS complex and the F1FO ATP synthase via Mic27 and Mic10","volume":"4","author":"Eydt","year":"2017","journal-title":"Microb. Cell (GrazAustria)"},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"1162","DOI":"10.1016\/j.jmb.2017.03.006","article-title":"Mic10, a Core Subunit of the Mitochondrial Contact Site and Cristae Organizing System, Interacts with the Dimeric F1Fo-ATP Synthase","volume":"429","author":"Rampelt","year":"2017","journal-title":"J. Mol. Biol."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"3399","DOI":"10.1038\/s41467-018-05655-x","article-title":"The cristae modulator Optic atrophy 1 requires mitochondrial ATP synthase oligomers to safeguard mitochondrial function","volume":"9","author":"Quirin","year":"2018","journal-title":"Nat. Commun."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"3309","DOI":"10.1002\/1873-3468.12384","article-title":"OPA1 functionally interacts with MIC60 but is dispensable for crista junction formation","volume":"590","author":"Barrera","year":"2016","journal-title":"FEBS Lett."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"424","DOI":"10.1016\/0014-4827(62)90194-5","article-title":"Fibrous Structures within the Matrix of Developing Chick Embryo Mitochondria","volume":"26","author":"Nass","year":"1962","journal-title":"Exp. Cell Res."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"593","DOI":"10.1083\/jcb.19.3.593","article-title":"Intramitochondrial Fibers with DNA Characteristics: I. Fixation and Electron Staining Reactions","volume":"19","author":"Nass","year":"1963","journal-title":"J. Cell Biol."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"613","DOI":"10.1083\/jcb.19.3.613","article-title":"Intramitochondrial Fibers with DNA Characteristics: II. Enzymatic and Other Hydrolytic Treatments","volume":"19","author":"Nass","year":"1963","journal-title":"J. Cell Biol."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"516","DOI":"10.1016\/0014-4827(65)90204-1","article-title":"The general occurrence of mitochondrial DNA","volume":"37","author":"Nass","year":"1965","journal-title":"Exp. Cell Res."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"1215","DOI":"10.1073\/pnas.56.4.1215","article-title":"The circularity of mitochondrial DNA","volume":"56","author":"Nass","year":"1966","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"521","DOI":"10.1016\/0022-2836(69)90240-X","article-title":"Mitochondrial DNA. I. Intramitochondrial distribution and structural relations of single- and double-length circular DNA","volume":"42","author":"Nass","year":"1969","journal-title":"J. Mol. Biol."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"1348","DOI":"10.1073\/pnas.74.4.1348","article-title":"Association of a protein structure of probable membrane derivation with HeLa cell mitochondrial DNA near its origin of replication","volume":"74","author":"Albring","year":"1977","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_72","doi-asserted-by":"crossref","unstructured":"Iborra, F.J., Kimura, H., and Cook, P.R. (2004). The functional organization of mitochondrial genomes in human cells. BMC Biol., 2.","DOI":"10.1186\/1741-7007-2-9"},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"6136","DOI":"10.1073\/pnas.1121558109","article-title":"Correlative 3D superresolution fluorescence and electron microscopy reveal the relationship of mitochondrial nucleoids to membranes","volume":"109","author":"Kopek","year":"2012","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"457","DOI":"10.1038\/290457a0","article-title":"Sequence and organization of the human mitochondrial genome","volume":"290","author":"Anderson","year":"1981","journal-title":"Nature"},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"393","DOI":"10.1016\/0092-8674(80)90350-5","article-title":"The tRNA genes punctuate the reading of genetic information in human mitochondrial DNA","volume":"22","author":"Ojala","year":"1980","journal-title":"Cell"},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"470","DOI":"10.1038\/290470a0","article-title":"tRNA punctuation model of RNA processing in human mitochondria","volume":"290","author":"Ojala","year":"1981","journal-title":"Nature"},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"1767","DOI":"10.1111\/febs.13981","article-title":"Human mitochondrial nucleases","volume":"284","author":"Bruni","year":"2017","journal-title":"FEBS J."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"2904","DOI":"10.4161\/cc.10.17.17060","article-title":"RNA processing in human mitochondria","volume":"10","author":"Sanchez","year":"2011","journal-title":"Cell Cycle"},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"679","DOI":"10.1146\/annurev.biochem.76.060305.152028","article-title":"DNA replication and transcription in mammalian mitochondria","volume":"76","author":"Falkenberg","year":"2007","journal-title":"Annu. Rev. Biochem."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1146\/annurev-biochem-060815-014402","article-title":"Maintenance and Expression of Mammalian Mitochondrial DNA","volume":"85","author":"Gustafsson","year":"2016","journal-title":"Annu. Rev. Biochem."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"388-388.e1","DOI":"10.1016\/j.cell.2017.12.039","article-title":"SnapShot: Mitochondrial Nucleoid","volume":"172","author":"Bonekamp","year":"2018","journal-title":"Cell"},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"16510","DOI":"10.1073\/pnas.1119738109","article-title":"Mammalian transcription factor A is a core component of the mitochondrial transcription machinery","volume":"109","author":"Shi","year":"2012","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"1290","DOI":"10.1038\/nsmb.2159","article-title":"The mitochondrial transcription and packaging factor Tfam imposes a U-turn on mitochondrial DNA","volume":"18","author":"Ngo","year":"2011","journal-title":"Nat. Struct. Mol. Biol."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"2653","DOI":"10.1242\/jcs.01134","article-title":"Organization and dynamics of human mitochondrial DNA","volume":"117","author":"Legros","year":"2004","journal-title":"J. Cell Sci."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"1117","DOI":"10.1083\/jcb.200712101","article-title":"Mitochondrial nucleoids maintain genetic autonomy but allow for functional complementation","volume":"181","author":"Gilkerson","year":"2008","journal-title":"J. Cell Biol."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"13534","DOI":"10.1073\/pnas.1109263108","article-title":"Super-resolution microscopy reveals that mammalian mitochondrial nucleoids have a uniform size and frequently contain a single copy of mtDNA","volume":"108","author":"Kukat","year":"2011","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"11288","DOI":"10.1073\/pnas.1512131112","article-title":"Cross-strand binding of TFAM to a single mtDNA molecule forms the mitochondrial nucleoid","volume":"112","author":"Kukat","year":"2015","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"1861","DOI":"10.1242\/jcs.028605","article-title":"Mitochondrial nucleoids undergo remodeling in response to metabolic cues","volume":"121","author":"Kucej","year":"2008","journal-title":"J. Cell Sci."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1038\/ng0398-231","article-title":"Mitochondrial transcription factor A is necessary for mtDNA maintenance and embryogenesis in mice","volume":"18","author":"Larsson","year":"1998","journal-title":"Nat. Genet."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1038\/5089","article-title":"Dilated cardiomyopathy and atrioventricular conduction blocks induced by heart-specific inactivation of mitochondrial DNA gene expression","volume":"21","author":"Wang","year":"1999","journal-title":"Nat. Genet."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"15066","DOI":"10.1073\/pnas.232591499","article-title":"Increased mitochondrial mass in mitochondrial myopathy mice","volume":"99","author":"Wredenberg","year":"2002","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"1325","DOI":"10.1073\/pnas.0605208103","article-title":"Progressive parkinsonism in mice with respiratory-chain-deficient dopamine neurons","volume":"104","author":"Ekstrand","year":"2007","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"515","DOI":"10.1038\/ng1769","article-title":"High levels of mitochondrial DNA deletions in substantia nigra neurons in aging and Parkinson disease","volume":"38","author":"Bender","year":"2006","journal-title":"Nat. Genet."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1016\/j.neuint.2018.04.013","article-title":"Mitochondrial alterations in Parkinson\u2019s disease human samples and cellular models","volume":"118","author":"Zilocchi","year":"2018","journal-title":"Neurochem. Int."},{"key":"ref_95","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_96","doi-asserted-by":"crossref","first-page":"1983","DOI":"10.1093\/hmg\/ddt051","article-title":"TWINKLE is an essential mitochondrial helicase required for synthesis of nascent D-loop strands and complete mtDNA replication","volume":"22","author":"Milenkovic","year":"2013","journal-title":"Hum. Mol. Genet."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"417","DOI":"10.1038\/nature02517","article-title":"Premature ageing in mice expressing defective mitochondrial DNA polymerase","volume":"429","author":"Trifunovic","year":"2004","journal-title":"Nature"},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"25791","DOI":"10.1074\/jbc.M604501200","article-title":"Human mitochondrial DNA nucleoids are linked to protein folding machinery and metabolic enzymes at the mitochondrial inner membrane","volume":"281","author":"Wang","year":"2006","journal-title":"J. Biol. Chem."},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"3665","DOI":"10.1074\/jbc.M708444200","article-title":"The layered structure of human mitochondrial DNA nucleoids","volume":"283","author":"Bogenhagen","year":"2008","journal-title":"J. Biol. Chem."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"988","DOI":"10.1016\/j.yexcr.2008.01.005","article-title":"Human prohibitin 1 maintains the organization and stability of the mitochondrial nucleoids","volume":"314","author":"Kasashima","year":"2008","journal-title":"Exp. Cell Res."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1083\/jcb.200609158","article-title":"The AAA+ protein ATAD3 has displacement loop binding properties and is involved in mitochondrial nucleoid organization","volume":"176","author":"He","year":"2007","journal-title":"J. Cell Biol."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"404","DOI":"10.1016\/j.chembiol.2017.02.002","article-title":"Proximity Biotinylation as a Method for Mapping Proteins Associated with mtDNA in Living Cells","volume":"24","author":"Han","year":"2017","journal-title":"Cell Chem. Biol."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"330","DOI":"10.1126\/science.39.1000.330","article-title":"Mitochondria in Tissue Culture","volume":"39","author":"Lewis","year":"1914","journal-title":"Science"},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"198","DOI":"10.1002\/jemt.1070270303","article-title":"Dynamics of mitochondria in living cells: Shape changes, dislocations, fusion, and fission of mitochondria","volume":"27","author":"Voth","year":"1994","journal-title":"Microsc. Res. Tech."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"1233","DOI":"10.1091\/mbc.8.7.1233","article-title":"Mitochondrial transmission during mating in Saccharomyces cerevisiae is determined by mitochondrial fusion and fission and the intramitochondrial segregation of mitochondrial DNA","volume":"8","author":"Nunnari","year":"1997","journal-title":"Mol. Biol. Cell"},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1146\/annurev.cellbio.14.1.265","article-title":"Mitochondrial dynamics in yeast","volume":"14","author":"Hermann","year":"1998","journal-title":"Annu. Rev. Cell Dev. Biol."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"178","DOI":"10.1016\/S0962-8924(01)02246-2","article-title":"Mitochondrial dynamics and division in budding yeast","volume":"12","author":"Shaw","year":"2002","journal-title":"Trends Cell Biol."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"1698","DOI":"10.1126\/science.1082192","article-title":"The division of endosymbiotic organelles","volume":"302","author":"Osteryoung","year":"2003","journal-title":"Science"},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"272","DOI":"10.1038\/90116","article-title":"Human cells are protected from mitochondrial dysfunction by complementation of DNA products in fused mitochondria","volume":"28","author":"Ono","year":"2001","journal-title":"Nat. Genet."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"872","DOI":"10.1038\/nrm3013","article-title":"Mitochondrial fusion and fission in cell life and death","volume":"11","author":"Westermann","year":"2010","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"621","DOI":"10.1083\/jcb.201609019","article-title":"Structures of human mitofusin 1 provide insight into mitochondrial tethering","volume":"215","author":"Qi","year":"2016","journal-title":"J. Cell Biol."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"858","DOI":"10.1126\/science.1099793","article-title":"Structural basis of mitochondrial tethering by mitofusin complexes","volume":"305","author":"Koshiba","year":"2004","journal-title":"Science"},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"233","DOI":"10.1038\/s41594-018-0034-8","article-title":"Structural basis for GTP hydrolysis and conformational change of MFN1 in mediating membrane fusion","volume":"25","author":"Yan","year":"2018","journal-title":"Nat. Struct. Mol. Biol."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"372","DOI":"10.1038\/nature21077","article-title":"MFN1 structures reveal nucleotide-triggered dimerization critical for mitochondrial fusion","volume":"542","author":"Cao","year":"2017","journal-title":"Nature"},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"1663","DOI":"10.1242\/jcs.115.8.1663","article-title":"Membrane topology and mitochondrial targeting of mitofusins, ubiquitous mammalian homologs of the transmembrane GTPase Fzo","volume":"115","author":"Rojo","year":"2002","journal-title":"J. Cell Sci."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1016\/j.ceb.2019.05.004","article-title":"The enigma of an interconnected mitochondrial reticulum: New insights into mitochondrial fusion","volume":"59","author":"Mattie","year":"2019","journal-title":"Curr. Opin. Cell Biol."},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"507","DOI":"10.1083\/jcb.201611194","article-title":"A new mitofusin topology places the redox-regulated C terminus in the mitochondrial intermembrane space","volume":"217","author":"Mattie","year":"2018","journal-title":"J. Cell Biol."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"449","DOI":"10.1038\/ng1341","article-title":"Mutations in the mitochondrial GTPase mitofusin 2 cause Charcot-Marie-Tooth neuropathy type 2A","volume":"36","author":"Zuchner","year":"2004","journal-title":"Nat. Genet."},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"2245","DOI":"10.1091\/mbc.12.8.2245","article-title":"Dynamin-related protein Drp1 is required for mitochondrial division in mammalian cells","volume":"12","author":"Smirnova","year":"2001","journal-title":"Mol. Biol. Cell"},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1083\/jcb.200211046","article-title":"Mitofusins Mfn1 and Mfn2 coordinately regulate mitochondrial fusion and are essential for embryonic development","volume":"160","author":"Chen","year":"2003","journal-title":"J. Cell Biol."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1146\/annurev.cellbio.22.010305.104638","article-title":"Mitochondrial fusion and fission in mammals","volume":"22","author":"Chan","year":"2006","journal-title":"Annu. Rev. Cell Dev. Biol."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1146\/annurev-genet-110410-132529","article-title":"Fusion and fission: Interlinked processes critical for mitochondrial health","volume":"46","author":"Chan","year":"2012","journal-title":"Annu. Rev. Genet."},{"key":"ref_123","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_124","first-page":"6","article-title":"Mechanisms of mitochondrial fission and fusion","volume":"5","author":"Shen","year":"2013","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"1747","DOI":"10.1126\/science.1100612","article-title":"Mitochondrial fusion intermediates revealed in vitro","volume":"305","author":"Meeusen","year":"2004","journal-title":"Science"},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"15927","DOI":"10.1073\/pnas.0407043101","article-title":"OPA1 requires mitofusin 1 to promote mitochondrial fusion","volume":"101","author":"Cipolat","year":"2004","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"515","DOI":"10.1016\/S1534-5807(01)00055-7","article-title":"The role of dynamin-related protein 1, a mediator of mitochondrial fission, in apoptosis","volume":"1","author":"Frank","year":"2001","journal-title":"Dev. Cell"},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"37972","DOI":"10.1074\/jbc.M606059200","article-title":"Proteolytic Processing of OPA1 Links Mitochondrial Dysfunction to Alterations in Mitochondrial Morphology","volume":"281","author":"Jagasia","year":"2006","journal-title":"J. Biol. Chem."},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1083\/jcb.200403022","article-title":"Alternative topogenesis of Mgm1 and mitochondrial morphology depend on ATP and a functional import motor","volume":"165","author":"Herlan","year":"2004","journal-title":"J. Cell Biol."},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"433","DOI":"10.1038\/sj.emboj.7601963","article-title":"Fission and selective fusion govern mitochondrial segregation and elimination by autophagy","volume":"27","author":"Twig","year":"2008","journal-title":"Embo J."},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1515\/hsz-2017-0206","article-title":"How to get rid of mitochondria: Crosstalk and regulation of multiple mitophagy pathways","volume":"399","author":"Zimmermann","year":"2017","journal-title":"Biol. Chem."},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"1070","DOI":"10.1042\/BST0321070","article-title":"Selective elimination of mitochondria from living cells induced by inhibitors of bioenergetic functions","volume":"32","author":"Lyamzaev","year":"2004","journal-title":"Biochem. Soc. Trans."},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"1141","DOI":"10.1083\/jcb.201007152","article-title":"Mff is an essential factor for mitochondrial recruitment of Drp1 during mitochondrial fission in mammalian cells","volume":"191","author":"Otera","year":"2010","journal-title":"J. Cell Biol."},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"531","DOI":"10.1083\/jcb.201508099","article-title":"Drp1-dependent mitochondrial fission via MiD49\/51 is essential for apoptotic cristae remodeling","volume":"212","author":"Otera","year":"2016","journal-title":"J. Cell Biol."},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"659","DOI":"10.1091\/mbc.e12-10-0721","article-title":"Fis1, Mff, MiD49, and MiD51 mediate Drp1 recruitment in mitochondrial fission","volume":"24","author":"Loson","year":"2013","journal-title":"Mol. Biol. Cell"},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1038\/nature20555","article-title":"Multiple dynamin family members collaborate to drive mitochondrial division","volume":"540","author":"Lee","year":"2016","journal-title":"Nature"},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"5239","DOI":"10.1038\/s41467-018-07543-w","article-title":"Dynamin-related protein 1 has membrane constricting and severing abilities sufficient for mitochondrial and peroxisomal fission","volume":"9","author":"Kamerkar","year":"2018","journal-title":"Nat. Commun."},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"E34","DOI":"10.1038\/s41586-019-1296-y","article-title":"Mitochondrial fission requires DRP1 but not dynamins","volume":"570","author":"Fonseca","year":"2019","journal-title":"Nature"},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"358","DOI":"10.1126\/science.1207385","article-title":"ER tubules mark sites of mitochondrial division","volume":"334","author":"Friedman","year":"2011","journal-title":"Science"},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"464","DOI":"10.1126\/science.1228360","article-title":"An actin-dependent step in mitochondrial fission mediated by the ER-associated formin INF2","volume":"339","author":"Korobova","year":"2013","journal-title":"Science"},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"2002","DOI":"10.1002\/ajmg.a.37721","article-title":"A novel de novo dominant negative mutation in DNM1L impairs mitochondrial fission and presents as childhood epileptic encephalopathy","volume":"170","author":"Fahrner","year":"2016","journal-title":"Am. J. Med Genet."},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"1603","DOI":"10.1002\/ajmg.a.37624","article-title":"Postnatal microcephaly and pain insensitivity due to a de novo heterozygous DNM1L mutation causing impaired mitochondrial fission and function","volume":"170","author":"Sheffer","year":"2016","journal-title":"Am. J. Med. Genet."},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"1736","DOI":"10.1056\/NEJMoa064436","article-title":"A lethal defect of mitochondrial and peroxisomal fission","volume":"356","author":"Waterham","year":"2007","journal-title":"N. Engl. J. Med."},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"380","DOI":"10.1101\/gad.6.3.380","article-title":"Mitochondrial DNA maintenance in yeast requires a protein containing a region related to the GTP-binding domain of dynamin","volume":"6","author":"Jones","year":"1992","journal-title":"Genes Dev."},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1007\/BF00324678","article-title":"Normal mitochondrial structure and genome maintenance in yeast requires the dynamin-like product of the MGM1 gene","volume":"24","author":"Guan","year":"1993","journal-title":"Curr. Genet."},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"359","DOI":"10.1083\/jcb.143.2.359","article-title":"Mitochondrial fusion in yeast requires the transmembrane GTPase Fzo1p","volume":"143","author":"Hermann","year":"1998","journal-title":"J. Cell Biol."},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"20150","DOI":"10.1074\/jbc.273.32.20150","article-title":"Fzo1p is a mitochondrial outer membrane protein essential for the biogenesis of functional mitochondria in Saccharomyces cerevisiae","volume":"273","author":"Rapaport","year":"1998","journal-title":"J. Biol. Chem."},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"1123","DOI":"10.1083\/jcb.152.6.1123","article-title":"UGO1 encodes an outer membrane protein required for mitochondrial fusion","volume":"152","author":"Sesaki","year":"2001","journal-title":"J. Cell Biol."},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"28298","DOI":"10.1074\/jbc.M401363200","article-title":"Ugo1p links the Fzo1p and Mgm1p GTPases for mitochondrial fusion","volume":"279","author":"Sesaki","year":"2004","journal-title":"J. Biol. Chem."},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"548","DOI":"10.1016\/j.cell.2007.06.026","article-title":"Mitochondrial fusion protects against neurodegeneration in the cerebellum","volume":"130","author":"Chen","year":"2007","journal-title":"Cell"},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"26185","DOI":"10.1074\/jbc.M503062200","article-title":"Disruption of fusion results in mitochondrial heterogeneity and dysfunction","volume":"280","author":"Chen","year":"2005","journal-title":"J. Biol. Chem."},{"key":"ref_152","doi-asserted-by":"crossref","first-page":"280","DOI":"10.1016\/j.cell.2010.02.026","article-title":"Mitochondrial fusion is required for mtDNA stability in skeletal muscle and tolerance of mtDNA mutations","volume":"141","author":"Chen","year":"2010","journal-title":"Cell"},{"key":"ref_153","doi-asserted-by":"crossref","first-page":"1327","DOI":"10.1161\/CIRCRESAHA.111.258723","article-title":"Mitochondrial fusion is essential for organelle function and cardiac homeostasis","volume":"109","author":"Chen","year":"2011","journal-title":"Circ. Res."},{"key":"ref_154","doi-asserted-by":"crossref","unstructured":"Silva Ramos, E., Motori, E., Bruser, C., Kuhl, I., Yeroslaviz, A., Ruzzenente, B., Kauppila, J.H.K., Busch, J.D., Hultenby, K., and Habermann, B.H. (2019). Mitochondrial fusion is required for regulation of mitochondrial DNA replication. PLoS Genet., 15.","DOI":"10.1371\/journal.pgen.1008085"},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"958","DOI":"10.1038\/ncb1907","article-title":"Mitochondrial fission factor Drp1 is essential for embryonic development and synapse formation in mice","volume":"11","author":"Ishihara","year":"2009","journal-title":"Nat. Cell Biol."},{"key":"ref_156","doi-asserted-by":"crossref","first-page":"805","DOI":"10.1083\/jcb.200903065","article-title":"The dynamin-related GTPase Drp1 is required for embryonic and brain development in mice","volume":"186","author":"Wakabayashi","year":"2009","journal-title":"J. Cell Biol."},{"key":"ref_157","doi-asserted-by":"crossref","unstructured":"Parone, P.A., Da Cruz, S., Tondera, D., Mattenberger, Y., James, D.I., Maechler, P., Barja, F., and Martinou, J.C. (2008). Preventing mitochondrial fission impairs mitochondrial function and leads to loss of mitochondrial DNA. PLoS ONE, 3.","DOI":"10.1371\/journal.pone.0003257"},{"key":"ref_158","doi-asserted-by":"crossref","first-page":"535","DOI":"10.1083\/jcb.201110034","article-title":"Mitochondrial division ensures the survival of postmitotic neurons by suppressing oxidative damage","volume":"197","author":"Kageyama","year":"2012","journal-title":"J. Cell Biol."},{"key":"ref_159","doi-asserted-by":"crossref","first-page":"11863","DOI":"10.1073\/pnas.1301951110","article-title":"Dynamics of nucleoid structure regulated by mitochondrial fission contributes to cristae reformation and release of cytochrome c","volume":"110","author":"Ishihara","year":"2013","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_160","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1128\/MCB.01054-14","article-title":"Dynamics of mitochondrial DNA nucleoids regulated by mitochondrial fission is essential for maintenance of homogeneously active mitochondria during neonatal heart development","volume":"35","author":"Ishihara","year":"2015","journal-title":"Mol. Cell. Biol."},{"key":"ref_161","doi-asserted-by":"crossref","first-page":"795","DOI":"10.1083\/jcb.201507035","article-title":"Titration of mitochondrial fusion rescues Mff-deficient cardiomyopathy","volume":"211","author":"Chen","year":"2015","journal-title":"J. Cell Biol."},{"key":"ref_162","doi-asserted-by":"crossref","first-page":"573","DOI":"10.1002\/1097-0029(20001215)51:6<573::AID-JEMT7>3.0.CO;2-2","article-title":"Yeast mitochondrial dynamics: Fusion, division, segregation, and shape","volume":"51","author":"Jensen","year":"2000","journal-title":"Microsc. Res. Tech."},{"key":"ref_163","doi-asserted-by":"crossref","first-page":"298","DOI":"10.1038\/13014","article-title":"The dynamin-related GTPase Dnm1 regulates mitochondrial fission in yeast","volume":"1","author":"Bleazard","year":"1999","journal-title":"Nat. Cell Biol."},{"key":"ref_164","doi-asserted-by":"crossref","first-page":"341","DOI":"10.1083\/jcb.151.2.341","article-title":"The dynamin-related GTPase, Mgm1p, is an intermembrane space protein required for maintenance of fusion competent mitochondria","volume":"151","author":"Wong","year":"2000","journal-title":"J. Cell Biol."},{"key":"ref_165","doi-asserted-by":"crossref","first-page":"aaf5549","DOI":"10.1126\/science.aaf5549","article-title":"ER-mitochondria contacts couple mtDNA synthesis with mitochondrial division in human cells","volume":"353","author":"Lewis","year":"2016","journal-title":"Science"},{"key":"ref_166","doi-asserted-by":"crossref","first-page":"966","DOI":"10.1212\/01.WNL.0000157282.76715.B1","article-title":"Mitochondrial DNA content is decreased in autosomal dominant optic atrophy","volume":"64","author":"Kim","year":"2005","journal-title":"Neurology"},{"key":"ref_167","doi-asserted-by":"crossref","first-page":"e003012","DOI":"10.1161\/JAHA.112.003012","article-title":"OPA1 mutation and late-onset cardiomyopathy: Mitochondrial dysfunction and mtDNA instability","volume":"1","author":"Chen","year":"2012","journal-title":"J. Am. Heart Assoc."},{"key":"ref_168","doi-asserted-by":"crossref","first-page":"1029","DOI":"10.1093\/brain\/awm005","article-title":"A splice site mutation in the murine Opa1 gene features pathology of autosomal dominant optic atrophy","volume":"130","author":"Alavi","year":"2007","journal-title":"Brain"},{"key":"ref_169","doi-asserted-by":"crossref","first-page":"1374","DOI":"10.1016\/j.cmet.2017.04.021","article-title":"Age-Associated Loss of OPA1 in Muscle Impacts Muscle Mass, Metabolic Homeostasis, Systemic Inflammation, and Epithelial Senescence","volume":"25","author":"Tezze","year":"2017","journal-title":"Cell Metab."},{"key":"ref_170","doi-asserted-by":"crossref","first-page":"160","DOI":"10.1016\/j.cell.2013.08.032","article-title":"Mitochondrial cristae shape determines respiratory chain supercomplexes assembly and respiratory efficiency","volume":"155","author":"Cogliati","year":"2013","journal-title":"Cell"},{"key":"ref_171","doi-asserted-by":"crossref","unstructured":"Romanello, V., Scalabrin, M., Albiero, M., Blaauw, B., Scorrano, L., and Sandri, M. (2019). Inhibition of the Fission Machinery Mitigates OPA1 Impairment in Adult Skeletal Muscles. Cells, 8.","DOI":"10.3390\/cells8060597"},{"key":"ref_172","doi-asserted-by":"crossref","first-page":"1543","DOI":"10.1091\/mbc.e04-08-0697","article-title":"The mitochondrial inner membrane protein mitofilin controls cristae morphology","volume":"16","author":"John","year":"2005","journal-title":"Mol. Biol. Cell"},{"key":"ref_173","doi-asserted-by":"crossref","first-page":"1842","DOI":"10.1091\/mbc.e13-03-0125","article-title":"Effects of Fcj1-Mos1 and mitochondrial division on aggregation of mitochondrial DNA nucleoids and organelle morphology","volume":"24","author":"Itoh","year":"2013","journal-title":"Mol. Biol. Cell"},{"key":"ref_174","first-page":"380","article-title":"Mic60\/Mitofilin determines MICOS assembly essential for mitochondrial dynamics and mtDNA nucleoid organization","volume":"22","author":"Li","year":"2015","journal-title":"Cell Death Differ."},{"key":"ref_175","doi-asserted-by":"crossref","first-page":"13990","DOI":"10.1074\/jbc.M512334200","article-title":"Mitochondrial membrane potential is dependent on the oligomeric state of F1F0-ATP synthase supracomplexes","volume":"281","author":"Bornhovd","year":"2006","journal-title":"J. Biol. Chem."},{"key":"ref_176","first-page":"R186","article-title":"Proteomic alterations of distinct mitochondrial subpopulations in the type 1 diabetic heart: Contribution of protein import dysfunction","volume":"300","author":"Baseler","year":"2011","journal-title":"Am. J. Physiol."},{"key":"ref_177","doi-asserted-by":"crossref","first-page":"212","DOI":"10.1016\/j.yjmcc.2014.11.008","article-title":"Transgenic overexpression of mitofilin attenuates diabetes mellitus-associated cardiac and mitochondria dysfunction","volume":"79","author":"Thapa","year":"2015","journal-title":"J. Mol. Cell. Cardiol."},{"key":"ref_178","doi-asserted-by":"crossref","first-page":"1177","DOI":"10.2741\/4541","article-title":"Mitochondrial DNA, mitochondrial dysfunction, and cardiac manifestations","volume":"22","author":"Lee","year":"2017","journal-title":"Front. Biosci."},{"key":"ref_179","doi-asserted-by":"crossref","first-page":"1501","DOI":"10.1016\/S0002-9440(10)65738-0","article-title":"Mitochondrial DNA mutations and mitochondrial abnormalities in dilated cardiomyopathy","volume":"153","author":"Arbustini","year":"1998","journal-title":"Am. J. Pathol."}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/20\/17\/4311\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T13:16:25Z","timestamp":1760188585000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/20\/17\/4311"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2019,9,3]]},"references-count":179,"journal-issue":{"issue":"17","published-online":{"date-parts":[[2019,9]]}},"alternative-id":["ijms20174311"],"URL":"https:\/\/doi.org\/10.3390\/ijms20174311","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2019,9,3]]}}}