{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T16:08:46Z","timestamp":1790784526510,"version":"4.1.0"},"reference-count":46,"publisher":"Pharmaceutical Society of Japan","issue":"8","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biological &amp; Pharmaceutical Bulletin","Biol. Pharm. Bull."],"published-print":{"date-parts":[[2019,8,1]]},"DOI":"10.1248\/bpb.b19-00316","type":"journal-article","created":{"date-parts":[[2019,7,31]],"date-time":"2019-07-31T22:03:32Z","timestamp":1564610612000},"page":"1394-1401","source":"Crossref","is-referenced-by-count":26,"title":["Reciprocal Regulation of Chaperone-Mediated Autophagy\/Microautophagy and Exosome Release"],"prefix":"10.1248","volume":"42","author":[{"given":"Mutsumi","family":"Oshima","sequence":"first","affiliation":[{"name":"Department of Chemico-Pharmacological Sciences, Graduate School of Pharmaceutical Sciences, Kumamoto University"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Takahiro","family":"Seki","sequence":"additional","affiliation":[{"name":"Department of Chemico-Pharmacological Sciences, Graduate School of Pharmaceutical Sciences, Kumamoto University"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yuki","family":"Kurauchi","sequence":"additional","affiliation":[{"name":"Department of Chemico-Pharmacological Sciences, Graduate School of Pharmaceutical Sciences, Kumamoto University"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Akinori","family":"Hisatsune","sequence":"additional","affiliation":[{"name":"Department of Chemico-Pharmacological Sciences, Graduate School of Pharmaceutical Sciences, Kumamoto University"},{"name":"Priority Organization for Innovation and Excellence, Kumamoto University"},{"name":"Program for Leading Graduate Schools \u201cHIGO (Health life science: Interdisciplinary and Glocal Oriented) Program,\u201d Kumamoto University"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hiroshi","family":"Katsuki","sequence":"additional","affiliation":[{"name":"Department of Chemico-Pharmacological Sciences, Graduate School of Pharmaceutical Sciences, Kumamoto University"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"163","reference":[{"key":"1","unstructured":"1) Tanaka K, Matsuda N. Proteostasis and neurodegeneration: the roles of proteasomal degradation and autophagy. <i>Biochim. Biophys. Acta.<\/i>, <b>1843<\/b>, 197\u2013204 (2014)."},{"key":"2","unstructured":"2) Haspel JA, Choi AMK. Autophagy: a core cellular process with emerging links to pulmonary disease. <i>Am. J. Respir. Crit. Care Med.<\/i>, <b>184<\/b>, 1237\u20131246 (2011)."},{"key":"3","unstructured":"3) Ciechanover A, Kwon YT. Degradation of misfolded proteins in neurodegenerative diseases: therapeutic targets and strategies. <i>Exp. Mol. Med.<\/i>, <b>47<\/b>, e147 (2015)."},{"key":"4","doi-asserted-by":"crossref","unstructured":"4) Smith DM. Could a common mechanism of protein degradation impairment underlie many neurodegenerative diseases? <i>J. Exp. Neurosci.<\/i>, <b>12<\/b>, 117906951879467 (2018).","DOI":"10.1177\/1179069518794675"},{"key":"5","unstructured":"5) Jackson MP, Hewitt EW. Cellular proteostasis: degradation of misfolded proteins by lysosomes. <i>Essays Biochem.<\/i>, <b>60<\/b>, 173\u2013180 (2016)."},{"key":"6","doi-asserted-by":"crossref","unstructured":"6) Hegde AN, Upadhya SC. Role of ubiquitin\u2013proteasome-mediated proteolysis in nervous system disease. <i>Biochim. Biophys. Acta<\/i>, <b>1809<\/b>, 128\u2013140 (2011).","DOI":"10.1016\/j.bbagrm.2010.07.006"},{"key":"7","doi-asserted-by":"crossref","unstructured":"7) Martinez-Vicente M. Autophagy in neurodegenerative diseases: from pathogenic dysfunction to therapeutic modulation. <i>Semin. Cell Dev. Biol.<\/i>, <b>40<\/b>, 115\u2013126 (2015).","DOI":"10.1016\/j.semcdb.2015.03.005"},{"key":"8","unstructured":"8) Wang Y, Martinez-Vicente M, Kr\u00fcger U, Kaushik S, Wong E, Mandelkow E-M, Cuervo AM, Mandelkow E. Tau fragmentation, aggregation and clearance: the dual role of lysosomal processing. <i>Hum. Mol. Genet.<\/i>, <b>18<\/b>, 4153\u20134170 (2009)."},{"key":"9","doi-asserted-by":"crossref","unstructured":"9) Campbell P, Morris H, Schapira A. Chaperone-mediated autophagy as a therapeutic target for Parkinson disease. <i>Expert Opin. Ther. Targets<\/i>, <b>22<\/b>, 823\u2013832 (2018).","DOI":"10.1080\/14728222.2018.1517156"},{"key":"10","doi-asserted-by":"crossref","unstructured":"10) Koga H, Martinez-Vicente M, Arias E, Kaushik S, Sulzer D, Cuervo AM. Constitutive upregulation of chaperone-mediated autophagy in huntington\u2019s disease. <i>J. Neurosci.<\/i>, <b>31<\/b>, 18492\u201318505 (2011).","DOI":"10.1523\/JNEUROSCI.3219-11.2011"},{"key":"11","doi-asserted-by":"crossref","unstructured":"11) Seki T, Yoshino KI, Tanaka S, Dohi E, Onji T, Yamamoto K, Hide I, Paulson HL, Saito N, Sakai N. Establishment of a novel fluorescence-based method to evaluate chaperone-mediated autophagy in a single neuron. <i>PLOS ONE<\/i>, <b>7<\/b>, e31232 (2012).","DOI":"10.1371\/journal.pone.0031232"},{"key":"12","doi-asserted-by":"crossref","unstructured":"12) Seki T, Sato M, Kibe Y, Ohta T, Oshima M, Konno A, Hirai H, Kurauchi Y, Hisatsune A, Katsuki H. Lysosomal dysfunction and early glial activation are involved in the pathogenesis of spinocerebellar ataxia type 21 caused by mutant transmembrane protein 240. <i>Neurobiol. Dis.<\/i>, <b>120<\/b>, 34\u201350 (2018).","DOI":"10.1016\/j.nbd.2018.08.022"},{"key":"13","doi-asserted-by":"crossref","unstructured":"13) Hasegawa M, Nonaka T, Masuda-Suzukake M. Prion-like mechanisms and potential therapeutic targets in neurodegenerative disorders. <i>Pharmacol. Ther.<\/i>, <b>172<\/b>, 22\u201333 (2017).","DOI":"10.1016\/j.pharmthera.2016.11.010"},{"key":"14","doi-asserted-by":"crossref","unstructured":"14) Jucker M, Walker LC. Propagation and spread of pathogenic protein assemblies in neurodegenerative diseases. <i>Nat. Neurosci.<\/i>, <b>21<\/b>, 1341\u20131349 (2018).","DOI":"10.1038\/s41593-018-0238-6"},{"key":"15","doi-asserted-by":"crossref","unstructured":"15) Lim Y-J, Lee S-J. Are exosomes the vehicle for protein aggregate propagation in neurodegenerative diseases? <i>Acta Neuropathol. Commun.<\/i>, <b>5<\/b>, 64 (2017).","DOI":"10.1186\/s40478-017-0467-z"},{"key":"16","doi-asserted-by":"crossref","unstructured":"16) Meldolesi J. Exosomes and ectosomes in intercellular communication. <i>Curr. Biol.<\/i>, <b>28<\/b>, R435\u2013R444 (2018).","DOI":"10.1016\/j.cub.2018.01.059"},{"key":"17","doi-asserted-by":"crossref","unstructured":"17) Gustafsson G, L\u00f6\u00f6v C, Persson E, L\u00e1zaro DF, Takeda S, Bergstr\u00f6m J, Erlandsson A, Sehlin D, Balaj L, Gy\u00f6rgy B, Hallbeck M, Outeiro TF, Breakefield XO, Hyman BT, Ingelsson M. Secretion and uptake of \u03b1-synuclein via extracellular vesicles in cultured cells. <i>Cell. Mol. Neurobiol.<\/i>, <b>38<\/b>, 1539\u20131550 (2018).","DOI":"10.1007\/s10571-018-0622-5"},{"key":"18","unstructured":"18) Basso M, Pozzi S, Tortarolo M, Fiordaliso F, Bisighini C, Pasetto L, Spaltro G, Lidonnici D, Gensano F, Battaglia E, Bendotti C, Bonetto V. Mutant copper-zinc superoxide dismutase (SOD1) induces protein secretion pathway alterations and exosome release in astrocytes: implications for disease spreading and motor neuron pathology in amyotrophic lateral sclerosis. <i>J. Biol. Chem.<\/i>, <b>288<\/b>, 15699\u201315711 (2013)."},{"key":"19","doi-asserted-by":"crossref","unstructured":"19) Iguchi Y, Eid L, Parent M, Soucy G, Bareil C, Riku Y, Kawai K, Takagi S, Yoshida M, Katsuno M, Sobue G, Julien J-P. Exosome secretion is a key pathway for clearance of pathological TDP-43. <i>Brain<\/i>, <b>139<\/b>, 3187\u20133201 (2016).","DOI":"10.1093\/brain\/aww237"},{"key":"20","doi-asserted-by":"crossref","unstructured":"20) Xu J, Camfield R, Gorski SM. The interplay between exosomes and autophagy-partners in crime. <i>J. Cell Sci.<\/i>, <b>131<\/b>, jcs215210 (2018).","DOI":"10.1242\/jcs.215210"},{"key":"21","doi-asserted-by":"crossref","unstructured":"21) Poehler A-M, Xiang W, Spitzer P, May VEL, Meixner H, Rockenstein E, Chutna O, Outeiro TF, Winkler J, Masliah E, Klucken J. Autophagy modulates SNCA\/\u03b1-synuclein release, thereby generating a hostile microenvironment. <i>Autophagy<\/i>, <b>10<\/b>, 2171\u20132192 (2014).","DOI":"10.4161\/auto.36436"},{"key":"22","doi-asserted-by":"crossref","unstructured":"22) Sahu R, Kaushik S, Clement CC, Cannizzo ES, Scharf B, Follenzi A, Potolicchio I, Nieves E, Cuervo AM, Santambrogio L. Microautophagy of cytosolic proteins by late endosomes. <i>Dev. Cell<\/i>, <b>20<\/b>, 131\u2013139 (2011).","DOI":"10.1016\/j.devcel.2010.12.003"},{"key":"23","unstructured":"23) Kaushik S, Cuervo AM. Chaperone-mediated autophagy: a unique way to enter the lysosome world. <i>Trends Cell. Biol.<\/i>, <b>22<\/b>, 407\u2013417 (2012)."},{"key":"24","doi-asserted-by":"crossref","unstructured":"24) Sato M, Seki T, Konno A, Hirai H, Kurauchi Y, Hisatsune A, Katsuki H. Fluorescent-based evaluation of chaperone-mediated autophagy and microautophagy activities in cultured cells. <i>Genes Cells<\/i>, <b>21<\/b>, 861\u2013873 (2016).","DOI":"10.1111\/gtc.12390"},{"key":"25","doi-asserted-by":"crossref","unstructured":"25) Nguyen B, Cohen M, Sad\u00e9e W. Guanine ribonucleotide depletion in mammalian cells. <i>Cancer Chemother. Pharmacol.<\/i>, <b>11<\/b>, 117\u2013119 (1983).","DOI":"10.1007\/BF00254259"},{"key":"26","doi-asserted-by":"crossref","unstructured":"26) Bandyopadhyay U, Sridhar S, Kaushik S, Kiffin R, Cuervo AM. Identification of regulators of chaperone-mediated autophagy. <i>Mol. Cell<\/i>, <b>39<\/b>, 535\u2013547 (2010).","DOI":"10.1016\/j.molcel.2010.08.004"},{"key":"27","unstructured":"27) Dowling RJO, Topisirovic I, Fonseca BD, Sonenberg N. Dissecting the role of mTOR: lessons from mTOR inhibitors. <i>Biochim. Biophys. Acta Proteins Proteomics<\/i>, <b>1804<\/b>, 433\u2013439 (2010)."},{"key":"28","doi-asserted-by":"crossref","unstructured":"28) Yang Y, Liang Z, Gu Z, Qin Z. Molecular mechanism and regulation of autophagy1. <i>Acta Pharmacol. Sin.<\/i>, <b>26<\/b>, 1421\u20131434 (2005).","DOI":"10.1111\/j.1745-7254.2005.00235.x"},{"key":"29","doi-asserted-by":"crossref","unstructured":"29) Rahman MA, Terasawa M, Mostofa MG, Ushimaru T. The TORC1\u2013Nem1\/Spo7\u2013Pah1\/lipin axis regulates microautophagy induction in budding yeast. <i>Biochem. Biophys. Res. Commun.<\/i>, <b>504<\/b>, 505\u2013512 (2018).","DOI":"10.1016\/j.bbrc.2018.09.011"},{"key":"30","doi-asserted-by":"crossref","unstructured":"30) Miller S, Oleksy A, Perisic O, Williams RL. Finding a fitting shoe for Cinderella. <i>Autophagy<\/i>, <b>6<\/b>, 805\u2013807 (2010).","DOI":"10.4161\/auto.6.6.12577"},{"key":"31","doi-asserted-by":"crossref","unstructured":"31) Ostrowski M, Carmo NB, Krumeich S, Fanget I, Raposo G, Savina A, Moita CF, Schauer K, Hume AN, Freitas RP, Goud B, Benaroch P, Hacohen N, Fukuda M, Desnos C, Seabra MC, Darchen F, Amigorena S, Moita LF, Thery C. Rab27a and Rab27b control different steps of the exosome secretion pathway. <i>Nat. Cell Biol.<\/i>, <b>12<\/b>, 19\u201330, 1\u201313 (2010).","DOI":"10.1038\/ncb2000"},{"key":"32","doi-asserted-by":"crossref","unstructured":"32) Mauvezin C, Nagy P, Juh\u00e1sz G, Neufeld TP. Autophagosome\u2013lysosome fusion is independent of V-ATPase-mediated acidification. <i>Nat. Commun.<\/i>, <b>6<\/b>, 7007 (2015).","DOI":"10.1038\/ncomms8007"},{"key":"33","doi-asserted-by":"crossref","unstructured":"33) Mauvezin C, Neufeld TP. Bafilomycin A1 disrupts autophagic flux by inhibiting both V-ATPase-dependent acidification and Ca-P60A\/SERCA-dependent autophagosome-lysosome fusion. <i>Autophagy<\/i>, <b>11<\/b>, 1437\u20131438 (2015).","DOI":"10.1080\/15548627.2015.1066957"},{"key":"34","doi-asserted-by":"crossref","unstructured":"34) Kajimoto T, Mohamed NNI, Badawy SMM, Matovelo SA, Hirase M, Nakamura S, Yoshida D, Okada T, Ijuin T, Nakamura S-I. Involvement of G\u03b2\u03b3 subunits of Gi protein coupled with S1P receptor on multivesicular endosomes in F-actin formation and cargo sorting into exosomes. <i>J. Biol. Chem.<\/i>, <b>293<\/b>, 245\u2013253 (2018).","DOI":"10.1074\/jbc.M117.808733"},{"key":"35","doi-asserted-by":"crossref","unstructured":"35) Abdulrahman BA, Abdelaziz DH, Schatzl HM. Autophagy regulates exosomal release of prions in neuronal cells. <i>J. Biol. Chem.<\/i>, <b>293<\/b>, 8956\u20138968 (2018).","DOI":"10.1074\/jbc.RA117.000713"},{"key":"36","doi-asserted-by":"crossref","unstructured":"36) Hikita T, Miyata M, Watanabe R, Oneyama C. Sensitive and rapid quantification of exosomes by fusing luciferase to exosome marker proteins. <i>Sci. Rep.<\/i>, <b>8<\/b>, 14035 (2018).","DOI":"10.1038\/s41598-018-32535-7"},{"key":"37","doi-asserted-by":"crossref","unstructured":"37) Villarroya-Beltri C, Baixauli F, Mittelbrunn M, Fern\u00e1ndez-Delgado I, Torralba D, Moreno-Gonzalo O, Baldanta S, Enrich C, Guerra S, S\u00e1nchez-Madrid F. ISGylation controls exosome secretion by promoting lysosomal degradation of MVB proteins. <i>Nat. Commun.<\/i>, <b>7<\/b>, 13588 (2016).","DOI":"10.1038\/ncomms13588"},{"key":"38","doi-asserted-by":"crossref","unstructured":"38) Henne WM, Buchkovich NJ, Emr SD. The ESCRT Pathway. <i>Dev. Cell<\/i>, <b>21<\/b>, 77\u201391 (2011).","DOI":"10.1016\/j.devcel.2011.05.015"},{"key":"39","doi-asserted-by":"crossref","unstructured":"39) Colombo M, Moita C, van Niel G, Kowal J, Vigneron J, Benaroch P, Manel N, Moita LF, Th\u00e9ry C, Raposo G. Analysis of ESCRT functions in exosome biogenesis, composition and secretion highlights the heterogeneity of extracellular vesicles. <i>J. Cell Sci.<\/i>, <b>126<\/b>, 5553\u20135565 (2013).","DOI":"10.1242\/jcs.128868"},{"key":"40","doi-asserted-by":"crossref","unstructured":"40) Catarino S, Pereira P, Gir\u00e3o H. Molecular control of chaperone-mediated autophagy. <i>Essays Biochem.<\/i>, <b>61<\/b>, 663\u2013674 (2017).","DOI":"10.1042\/EBC20170057"},{"key":"41","doi-asserted-by":"crossref","unstructured":"41) Alvarez-Erviti L, Seow Y, Schapira AH, Gardiner C, Sargent IL, Wood MJA, Cooper JM. Lysosomal dysfunction increases exosome-mediated alpha-synuclein release and transmission. <i>Neurobiol. Dis.<\/i>, <b>42<\/b>, 360\u2013367 (2011).","DOI":"10.1016\/j.nbd.2011.01.029"},{"key":"42","doi-asserted-by":"crossref","unstructured":"42) Fussi N, H\u00f6llerhage M, Chakroun T, Nyk\u00e4nen N-P, R\u00f6sler TW, Koeglsperger T, Wurst W, Behrends C, H\u00f6glinger GU. Exosomal secretion of \u03b1-synuclein as protective mechanism after upstream blockage of macroautophagy. <i>Cell Death Dis.<\/i>, <b>9<\/b>, 757 (2018).","DOI":"10.1038\/s41419-018-0816-2"},{"key":"43","unstructured":"43) Li W, Nie T, Xu H, Yang J, Yang Q, Mao Z. Chaperone-mediated autophagy: Advances from bench to bedside. <i>Neurobiol. Dis.<\/i>, <b>122<\/b>, 41\u201348 (2019)."},{"key":"44","doi-asserted-by":"crossref","unstructured":"44) Kubo Y, Masumoto H, Izumida M, Kakoki K, Hayashi H, Matsuyama T. Rab3a-bound CD63 is degraded and Rab3a-Free CD63 is incorporated into HIV-1 particles. <i>Front. Microbiol.<\/i>, <b>8<\/b>, 1653 (2017).","DOI":"10.3389\/fmicb.2017.01653"},{"key":"45","doi-asserted-by":"crossref","unstructured":"45) Howitt J, Hill AF. Exosomes in the pathology of neurodegenerative diseases. <i>J. Biol. Chem.<\/i>, <b>291<\/b>, 26589\u201326597 (2016).","DOI":"10.1074\/jbc.R116.757955"},{"key":"46","doi-asserted-by":"crossref","unstructured":"46) Desd\u00edn-Mic\u00f3 G, Mittelbrunn M. Role of exosomes in the protection of cellular homeostasis. <i>Cell Adh. Migr.<\/i>, <b>11<\/b>, 127\u2013134 (2017).","DOI":"10.1080\/19336918.2016.1251000"}],"container-title":["Biological and Pharmaceutical Bulletin"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.jstage.jst.go.jp\/article\/bpb\/42\/8\/42_b19-00316\/_pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2019,8,3]],"date-time":"2019-08-03T03:23:57Z","timestamp":1564802637000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.jstage.jst.go.jp\/article\/bpb\/42\/8\/42_b19-00316\/_article"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2019,8,1]]},"references-count":46,"journal-issue":{"issue":"8","published-print":{"date-parts":[[2019]]}},"URL":"https:\/\/doi.org\/10.1248\/bpb.b19-00316","relation":{},"ISSN":["0918-6158","1347-5215"],"issn-type":[{"value":"0918-6158","type":"print"},{"value":"1347-5215","type":"electronic"}],"subject":[],"published":{"date-parts":[[2019,8,1]]}}}