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Volumn 17, Issue 3, 2016, Pages 300-316

The ubiquitin signal and autophagy: An orchestrated dance leading to mitochondrial degradation

Author keywords

mitochondria; mitophagy; Parkin; Parkinson's disease; PINK1

Indexed keywords

PARKIN; PINK1 PROTEIN; UBIQUITIN; UNCLASSIFIED DRUG; PROTEIN KINASE; PTEN-INDUCED PUTATIVE KINASE;

EID: 84959481890     PISSN: 1469221X     EISSN: 14693178     Source Type: Journal    
DOI: 10.15252/embr.201541486     Document Type: Review
Times cited : (192)

References (179)
  • 1
    • 27544466847 scopus 로고    scopus 로고
    • Mitochondrial morphology and dynamics in yeast and multicellular eukaryotes
    • Okamoto K, Shaw JM, (2005) Mitochondrial morphology and dynamics in yeast and multicellular eukaryotes. Annu Rev Genet 39: 503-536
    • (2005) Annu Rev Genet , vol.39 , pp. 503-536
    • Okamoto, K.1    Shaw, J.M.2
  • 2
    • 38549101188 scopus 로고    scopus 로고
    • Quality control of mitochondria: Protection against neurodegeneration and ageing
    • Tatsuta T, Langer T, (2008) Quality control of mitochondria: protection against neurodegeneration and ageing. EMBO J 27: 306-314
    • (2008) EMBO J , vol.27 , pp. 306-314
    • Tatsuta, T.1    Langer, T.2
  • 3
    • 73049129373 scopus 로고
    • The L-3,4-dioxyphenylalanine (DOPA)-effect in Parkinson-akinesia
    • Birkmayer W, Hornykiewicz O, (1961) The L-3,4-dioxyphenylalanine (DOPA)-effect in Parkinson-akinesia. Wien Klin Wochenschr 73: 787-788
    • (1961) Wien Klin Wochenschr , vol.73 , pp. 787-788
    • Birkmayer, W.1    Hornykiewicz, O.2
  • 4
    • 0032568534 scopus 로고    scopus 로고
    • Alpha-Synuclein in filamentous inclusions of Lewy bodies from Parkinson's disease and dementia with Lewy bodies
    • Spillantini MG, Crowther RA, Jakes R, Hasegawa M, Goedert M, (1998) Alpha-Synuclein in filamentous inclusions of Lewy bodies from Parkinson's disease and dementia with Lewy bodies. Proc Natl Acad Sci USA 95: 6469-6473
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 6469-6473
    • Spillantini, M.G.1    Crowther, R.A.2    Jakes, R.3    Hasegawa, M.4    Goedert, M.5
  • 5
    • 84922309470 scopus 로고    scopus 로고
    • SnapShot: Genetics of Parkinson's disease
    • e571
    • Bras J, Guerreiro R, Hardy J, (2015) SnapShot: genetics of Parkinson's disease. Cell 160: 570-570 e571
    • (2015) Cell , vol.160 , pp. 570
    • Bras, J.1    Guerreiro, R.2    Hardy, J.3
  • 6
    • 84921369563 scopus 로고    scopus 로고
    • The roles of PINK1, parkin, and mitochondrial fidelity in Parkinson's disease
    • Pickrell AM, Youle RJ, (2015) The roles of PINK1, parkin, and mitochondrial fidelity in Parkinson's disease. Neuron 85: 257-273
    • (2015) Neuron , vol.85 , pp. 257-273
    • Pickrell, A.M.1    Youle, R.J.2
  • 9
    • 0034680913 scopus 로고    scopus 로고
    • Parkin suppresses unfolded protein stress-induced cell death through its E3 ubiquitin-protein ligase activity
    • Imai Y, Soda M, Takahashi R, (2000) Parkin suppresses unfolded protein stress-induced cell death through its E3 ubiquitin-protein ligase activity. J Biol Chem 275: 35661-35664
    • (2000) J Biol Chem , vol.275 , pp. 35661-35664
    • Imai, Y.1    Soda, M.2    Takahashi, R.3
  • 10
    • 0034700158 scopus 로고    scopus 로고
    • Parkin functions as an E2-dependent ubiquitin- protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1
    • Zhang Y, Gao J, Chung KK, Huang H, Dawson VL, Dawson TM, (2000) Parkin functions as an E2-dependent ubiquitin- protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1. Proc Natl Acad Sci USA 97: 13354-13359
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 13354-13359
    • Zhang, Y.1    Gao, J.2    Chung, K.K.3    Huang, H.4    Dawson, V.L.5    Dawson, T.M.6
  • 14
    • 33644543761 scopus 로고    scopus 로고
    • Expanding insights of mitochondrial dysfunction in Parkinson's disease
    • Abou-Sleiman PM, Muqit MM, Wood NW, (2006) Expanding insights of mitochondrial dysfunction in Parkinson's disease. Nat Rev Neurosci 7: 207-219
    • (2006) Nat Rev Neurosci , vol.7 , pp. 207-219
    • Abou-Sleiman, P.M.1    Muqit, M.M.2    Wood, N.W.3
  • 15
    • 0020680904 scopus 로고
    • Chronic Parkinsonism in humans due to a product of meperidine-analog synthesis
    • Langston JW, Ballard P, Tetrud JW, Irwin I, (1983) Chronic Parkinsonism in humans due to a product of meperidine-analog synthesis. Science 219: 979-980
    • (1983) Science , vol.219 , pp. 979-980
    • Langston, J.W.1    Ballard, P.2    Tetrud, J.W.3    Irwin, I.4
  • 20
    • 84890031660 scopus 로고    scopus 로고
    • The mitochondrial disulfide relay system: Roles in oxidative protein folding and beyond
    • Fischer M, Riemer J, (2013) The mitochondrial disulfide relay system: roles in oxidative protein folding and beyond. Int J Cell Biol 2013: 742923
    • (2013) Int J Cell Biol , vol.2013 , pp. 742923
    • Fischer, M.1    Riemer, J.2
  • 24
    • 33746080412 scopus 로고    scopus 로고
    • Mitochondrial pathology and muscle and dopaminergic neuron degeneration caused by inactivation of Drosophila Pink1 is rescued by Parkin
    • Yang Y, Gehrke S, Imai Y, Huang Z, Ouyang Y, Wang JW, Yang L, Beal MF, Vogel H, Lu B, (2006) Mitochondrial pathology and muscle and dopaminergic neuron degeneration caused by inactivation of Drosophila Pink1 is rescued by Parkin. Proc Natl Acad Sci USA 103: 10793-10798
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 10793-10798
    • Yang, Y.1    Gehrke, S.2    Imai, Y.3    Huang, Z.4    Ouyang, Y.5    Wang, J.W.6    Yang, L.7    Beal, M.F.8    Vogel, H.9    Lu, B.10
  • 26
    • 0035292759 scopus 로고    scopus 로고
    • Themes and variations on ubiquitylation
    • Weissman AM, (2001) Themes and variations on ubiquitylation. Nat Rev Mol Cell Biol 2: 169-178
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 169-178
    • Weissman, A.M.1
  • 27
    • 9744227183 scopus 로고    scopus 로고
    • Ubiquitin: Structures, functions, mechanisms
    • Pickart CM, Eddins MJ, (2004) Ubiquitin: structures, functions, mechanisms. Biochim Biophys Acta 1695: 55-72
    • (2004) Biochim Biophys Acta , vol.1695 , pp. 55-72
    • Pickart, C.M.1    Eddins, M.J.2
  • 30
    • 34548851476 scopus 로고    scopus 로고
    • Parkin-mediated K63-linked polyubiquitination targets misfolded DJ-1 to aggresomes via binding to HDAC6
    • Olzmann JA, Li L, Chudaev MV, Chen J, Perez FA, Palmiter RD, Chin LS, (2007) Parkin-mediated K63-linked polyubiquitination targets misfolded DJ-1 to aggresomes via binding to HDAC6. J Cell Biol 178: 1025-1038
    • (2007) J Cell Biol , vol.178 , pp. 1025-1038
    • Olzmann, J.A.1    Li, L.2    Chudaev, M.V.3    Chen, J.4    Perez, F.A.5    Palmiter, R.D.6    Chin, L.S.7
  • 31
    • 38349114036 scopus 로고    scopus 로고
    • Lysine 63-linked ubiquitination promotes the formation and autophagic clearance of protein inclusions associated with neurodegenerative diseases
    • Tan JM, Wong ES, Kirkpatrick DS, Pletnikova O, Ko HS, Tay SP, Ho MW, Troncoso J, Gygi SP, Lee MK, et al, (2008) Lysine 63-linked ubiquitination promotes the formation and autophagic clearance of protein inclusions associated with neurodegenerative diseases. Hum Mol Genet 17: 431-439
    • (2008) Hum Mol Genet , vol.17 , pp. 431-439
    • Tan, J.M.1    Wong, E.S.2    Kirkpatrick, D.S.3    Pletnikova, O.4    Ko, H.S.5    Tay, S.P.6    Ho, M.W.7    Troncoso, J.8    Gygi, S.P.9    Lee, M.K.10
  • 32
    • 0034327504 scopus 로고    scopus 로고
    • Ubiquitin in chains
    • Pickart CM, (2000) Ubiquitin in chains. Trends Biochem Sci 25: 544-548
    • (2000) Trends Biochem Sci , vol.25 , pp. 544-548
    • Pickart, C.M.1
  • 34
    • 79957949190 scopus 로고    scopus 로고
    • UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids
    • Wenzel DM, Lissounov A, Brzovic PS, Klevit RE, (2011) UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids. Nature 474: 105-108
    • (2011) Nature , vol.474 , pp. 105-108
    • Wenzel, D.M.1    Lissounov, A.2    Brzovic, P.S.3    Klevit, R.E.4
  • 35
    • 58149314211 scopus 로고    scopus 로고
    • Parkin is recruited selectively to impaired mitochondria and promotes their autophagy
    • Narendra D, Tanaka A, Suen DF, Youle RJ, (2008) Parkin is recruited selectively to impaired mitochondria and promotes their autophagy. J Cell Biol 183: 795-803
    • (2008) J Cell Biol , vol.183 , pp. 795-803
    • Narendra, D.1    Tanaka, A.2    Suen, D.F.3    Youle, R.J.4
  • 36
    • 77951181836 scopus 로고    scopus 로고
    • PINK1 stabilized by mitochondrial depolarization recruits Parkin to damaged mitochondria and activates latent Parkin for mitophagy
    • Matsuda N, Sato S, Shiba K, Okatsu K, Saisho K, Gautier CA, Sou YS, Saiki S, Kawajiri S, Sato F, et al, (2010) PINK1 stabilized by mitochondrial depolarization recruits Parkin to damaged mitochondria and activates latent Parkin for mitophagy. J Cell Biol 189: 211-221
    • (2010) J Cell Biol , vol.189 , pp. 211-221
    • Matsuda, N.1    Sato, S.2    Shiba, K.3    Okatsu, K.4    Saisho, K.5    Gautier, C.A.6    Sou, Y.S.7    Saiki, S.8    Kawajiri, S.9    Sato, F.10
  • 39
    • 0035057837 scopus 로고    scopus 로고
    • Control of mitochondrial morphology by a human mitofusin
    • Santel A, Fuller MT, (2001) Control of mitochondrial morphology by a human mitofusin. J Cell Sci 114: 867-874
    • (2001) J Cell Sci , vol.114 , pp. 867-874
    • Santel, A.1    Fuller, M.T.2
  • 40
    • 79957472437 scopus 로고    scopus 로고
    • Parkin mediates proteasome-dependent protein degradation and rupture of the outer mitochondrial membrane
    • Yoshii SR, Kishi C, Ishihara N, Mizushima N, (2011) Parkin mediates proteasome-dependent protein degradation and rupture of the outer mitochondrial membrane. J Biol Chem 286: 19630-19640
    • (2011) J Biol Chem , vol.286 , pp. 19630-19640
    • Yoshii, S.R.1    Kishi, C.2    Ishihara, N.3    Mizushima, N.4
  • 43
    • 84907059487 scopus 로고    scopus 로고
    • The VCP/p97 system at a glance: Connecting cellular function to disease pathogenesis
    • Meyer H, Weihl CC, (2014) The VCP/p97 system at a glance: connecting cellular function to disease pathogenesis. J Cell Sci 127: 3877-3883
    • (2014) J Cell Sci , vol.127 , pp. 3877-3883
    • Meyer, H.1    Weihl, C.C.2
  • 44
    • 84942293377 scopus 로고    scopus 로고
    • Control of p97 function by cofactor binding
    • Buchberger A, Schindelin H, Hanzelmann P, (2015) Control of p97 function by cofactor binding. FEBS Lett 589: 2578-2589
    • (2015) FEBS Lett , vol.589 , pp. 2578-2589
    • Buchberger, A.1    Schindelin, H.2    Hanzelmann, P.3
  • 45
    • 84888356138 scopus 로고    scopus 로고
    • Different dynamic movements of wild-type and pathogenic VCPs and their cofactors to damaged mitochondria in a Parkin-mediated mitochondrial quality control system
    • Kimura Y, Fukushi J, Hori S, Matsuda N, Okatsu K, Kakiyama Y, Kawawaki J, Kakizuka A, Tanaka K, (2013) Different dynamic movements of wild-type and pathogenic VCPs and their cofactors to damaged mitochondria in a Parkin-mediated mitochondrial quality control system. Genes Cells 18: 1131-1143
    • (2013) Genes Cells , vol.18 , pp. 1131-1143
    • Kimura, Y.1    Fukushi, J.2    Hori, S.3    Matsuda, N.4    Okatsu, K.5    Kakiyama, Y.6    Kawawaki, J.7    Kakizuka, A.8    Tanaka, K.9
  • 48
    • 84868575932 scopus 로고    scopus 로고
    • Mitochondrial quality control mediated by PINK1 and Parkin: Links to parkinsonism
    • Narendra D, Walker JE, Youle R, (2012) Mitochondrial quality control mediated by PINK1 and Parkin: links to parkinsonism. Cold Spring Harb Perspect Biol 4: a011338
    • (2012) Cold Spring Harb Perspect Biol , vol.4 , pp. a011338
    • Narendra, D.1    Walker, J.E.2    Youle, R.3
  • 50
    • 78649463381 scopus 로고    scopus 로고
    • Mitofusin 1 and mitofusin 2 are ubiquitinated in a PINK1/parkin-dependent manner upon induction of mitophagy
    • Gegg ME, Cooper JM, Chau KY, Rojo M, Schapira AH, Taanman JW, (2010) Mitofusin 1 and mitofusin 2 are ubiquitinated in a PINK1/parkin-dependent manner upon induction of mitophagy. Hum Mol Genet 19: 4861-4870
    • (2010) Hum Mol Genet , vol.19 , pp. 4861-4870
    • Gegg, M.E.1    Cooper, J.M.2    Chau, K.Y.3    Rojo, M.4    Schapira, A.H.5    Taanman, J.W.6
  • 51
    • 77955844260 scopus 로고    scopus 로고
    • The mitochondrial fusion-promoting factor mitofusin is a substrate of the PINK1/parkin pathway
    • Poole AC, Thomas RE, Yu S, Vincow ES, Pallanck L, (2010) The mitochondrial fusion-promoting factor mitofusin is a substrate of the PINK1/parkin pathway. PLoS ONE 5: e10054
    • (2010) PLoS ONE , vol.5 , pp. e10054
    • Poole, A.C.1    Thomas, R.E.2    Yu, S.3    Vincow, E.S.4    Pallanck, L.5
  • 52
  • 54
    • 77952326081 scopus 로고    scopus 로고
    • Disease-causing mutations in parkin impair mitochondrial ubiquitination, aggregation, and HDAC6-dependent mitophagy
    • Lee JY, Nagano Y, Taylor JP, Lim KL, Yao TP, (2010) Disease-causing mutations in parkin impair mitochondrial ubiquitination, aggregation, and HDAC6-dependent mitophagy. J Cell Biol 189: 671-679
    • (2010) J Cell Biol , vol.189 , pp. 671-679
    • Lee, J.Y.1    Nagano, Y.2    Taylor, J.P.3    Lim, K.L.4    Yao, T.P.5
  • 57
    • 84857032953 scopus 로고    scopus 로고
    • Role of PINK1 binding to the TOM complex and alternate intracellular membranes in recruitment and activation of the E3 ligase Parkin
    • Lazarou M, Jin SM, Kane LA, Youle RJ, (2012) Role of PINK1 binding to the TOM complex and alternate intracellular membranes in recruitment and activation of the E3 ligase Parkin. Dev Cell 22: 320-333
    • (2012) Dev Cell , vol.22 , pp. 320-333
    • Lazarou, M.1    Jin, S.M.2    Kane, L.A.3    Youle, R.J.4
  • 58
    • 70349451660 scopus 로고    scopus 로고
    • Multiple pathways for mitochondrial protein traffic
    • Endo T, Yamano K, (2009) Multiple pathways for mitochondrial protein traffic. Biol Chem 390: 723-730
    • (2009) Biol Chem , vol.390 , pp. 723-730
    • Endo, T.1    Yamano, K.2
  • 61
    • 84890957474 scopus 로고    scopus 로고
    • A dimeric PINK1-containing complex on depolarized mitochondria stimulates Parkin recruitment
    • Okatsu K, Uno M, Koyano F, Go E, Kimura M, Oka T, Tanaka K, Matsuda N, (2013) A dimeric PINK1-containing complex on depolarized mitochondria stimulates Parkin recruitment. J Biol Chem 288: 36372-36384
    • (2013) J Biol Chem , vol.288 , pp. 36372-36384
    • Okatsu, K.1    Uno, M.2    Koyano, F.3    Go, E.4    Kimura, M.5    Oka, T.6    Tanaka, K.7    Matsuda, N.8
  • 62
    • 84866072587 scopus 로고    scopus 로고
    • PINK1 autophosphorylation upon membrane potential dissipation is essential for Parkin recruitment to damaged mitochondria
    • Okatsu K, Oka T, Iguchi M, Imamura K, Kosako H, Tani N, Kimura M, Go E, Koyano F, Funayama M, et al, (2012) PINK1 autophosphorylation upon membrane potential dissipation is essential for Parkin recruitment to damaged mitochondria. Nat Commun 3: 1016
    • (2012) Nat Commun , vol.3 , pp. 1016
    • Okatsu, K.1    Oka, T.2    Iguchi, M.3    Imamura, K.4    Kosako, H.5    Tani, N.6    Kimura, M.7    Go, E.8    Koyano, F.9    Funayama, M.10
  • 63
    • 84921925390 scopus 로고    scopus 로고
    • PINK1 kinase catalytic activity is regulated by phosphorylation on serines 228 and 402
    • Aerts L, Craessaerts K, De Strooper B, Morais VA, (2015) PINK1 kinase catalytic activity is regulated by phosphorylation on serines 228 and 402. J Biol Chem 290: 2798-2811
    • (2015) J Biol Chem , vol.290 , pp. 2798-2811
    • Aerts, L.1    Craessaerts, K.2    De Strooper, B.3    Morais, V.A.4
  • 64
    • 84922820920 scopus 로고    scopus 로고
    • Unconventional PINK1 localization to the outer membrane of depolarized mitochondria drives Parkin recruitment
    • Okatsu K, Kimura M, Oka T, Tanaka K, Matsuda N, (2015) Unconventional PINK1 localization to the outer membrane of depolarized mitochondria drives Parkin recruitment. J Cell Sci 128: 964-978
    • (2015) J Cell Sci , vol.128 , pp. 964-978
    • Okatsu, K.1    Kimura, M.2    Oka, T.3    Tanaka, K.4    Matsuda, N.5
  • 65
    • 84873045973 scopus 로고    scopus 로고
    • PINK1 drives Parkin self-association and HECT-like E3 activity upstream of mitochondrial binding
    • Lazarou M, Narendra DP, Jin SM, Tekle E, Banerjee S, Youle RJ, (2013) PINK1 drives Parkin self-association and HECT-like E3 activity upstream of mitochondrial binding. J Cell Biol 200: 163-172
    • (2013) J Cell Biol , vol.200 , pp. 163-172
    • Lazarou, M.1    Narendra, D.P.2    Jin, S.M.3    Tekle, E.4    Banerjee, S.5    Youle, R.J.6
  • 66
    • 84879885169 scopus 로고    scopus 로고
    • Parkin mitochondrial translocation is achieved through a novel catalytic activity coupled mechanism
    • Zheng X, Hunter T, (2013) Parkin mitochondrial translocation is achieved through a novel catalytic activity coupled mechanism. Cell Res 23: 886-897
    • (2013) Cell Res , vol.23 , pp. 886-897
    • Zheng, X.1    Hunter, T.2
  • 68
    • 84871891737 scopus 로고    scopus 로고
    • PINK1-mediated phosphorylation of the Parkin ubiquitin-like domain primes mitochondrial translocation of Parkin and regulates mitophagy
    • Shiba-Fukushima K, Imai Y, Yoshida S, Ishihama Y, Kanao T, Sato S, Hattori N, (2012) PINK1-mediated phosphorylation of the Parkin ubiquitin-like domain primes mitochondrial translocation of Parkin and regulates mitophagy. Sci Rep 2: 1002
    • (2012) Sci Rep , vol.2 , pp. 1002
    • Shiba-Fukushima, K.1    Imai, Y.2    Yoshida, S.3    Ishihama, Y.4    Kanao, T.5    Sato, S.6    Hattori, N.7
  • 76
    • 84940783815 scopus 로고    scopus 로고
    • Expanding the ubiquitin code through post-translational modification
    • Herhaus L, Dikic I, (2015) Expanding the ubiquitin code through post-translational modification. EMBO Rep 16: 1071-1083
    • (2015) EMBO Rep , vol.16 , pp. 1071-1083
    • Herhaus, L.1    Dikic, I.2
  • 77
    • 84905384868 scopus 로고    scopus 로고
    • Pink1, the first ubiquitin kinase
    • Zheng X, Hunter T, (2014) Pink1, the first ubiquitin kinase. EMBO J 33: 1621-1623
    • (2014) EMBO J , vol.33 , pp. 1621-1623
    • Zheng, X.1    Hunter, T.2
  • 83
    • 33750302074 scopus 로고    scopus 로고
    • Endocytosis: The DUB version
    • Clague MJ, Urbe S, (2006) Endocytosis: the DUB version. Trends Cell Biol 16: 551-559
    • (2006) Trends Cell Biol , vol.16 , pp. 551-559
    • Clague, M.J.1    Urbe, S.2
  • 87
    • 84881477223 scopus 로고    scopus 로고
    • Structure of the human Parkin ligase domain in an autoinhibited state
    • Wauer T, Komander D, (2013) Structure of the human Parkin ligase domain in an autoinhibited state. EMBO J 32: 2099-2112
    • (2013) EMBO J , vol.32 , pp. 2099-2112
    • Wauer, T.1    Komander, D.2
  • 93
    • 84939795423 scopus 로고    scopus 로고
    • Mechanism of phospho-ubiquitin-induced PARKIN activation
    • Wauer T, Simicek M, Schubert A, Komander D, (2015) Mechanism of phospho-ubiquitin-induced PARKIN activation. Nature 524: 370-374
    • (2015) Nature , vol.524 , pp. 370-374
    • Wauer, T.1    Simicek, M.2    Schubert, A.3    Komander, D.4
  • 94
  • 96
    • 84878931274 scopus 로고    scopus 로고
    • PINK1 rendered temperature sensitive by disease-associated and engineered mutations
    • Narendra DP, Wang C, Youle RJ, Walker JE, (2013) PINK1 rendered temperature sensitive by disease-associated and engineered mutations. Hum Mol Genet 22: 2572-2589
    • (2013) Hum Mol Genet , vol.22 , pp. 2572-2589
    • Narendra, D.P.1    Wang, C.2    Youle, R.J.3    Walker, J.E.4
  • 97
    • 17644365438 scopus 로고    scopus 로고
    • Mutations in PTEN-induced putative kinase 1 associated with recessive parkinsonism have differential effects on protein stability
    • Beilina A, Van Der Brug M, Ahmad R, Kesavapany S, Miller DW, Petsko GA, Cookson MR, (2005) Mutations in PTEN-induced putative kinase 1 associated with recessive parkinsonism have differential effects on protein stability. Proc Natl Acad Sci USA 102: 5703-5708
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 5703-5708
    • Beilina, A.1    Van Der Brug, M.2    Ahmad, R.3    Kesavapany, S.4    Miller, D.W.5    Petsko, G.A.6    Cookson, M.R.7
  • 99
    • 78649685455 scopus 로고    scopus 로고
    • Mitochondrial membrane potential regulates PINK1 import and proteolytic destabilization by PARL
    • Jin SM, Lazarou M, Wang C, Kane LA, Narendra DP, Youle RJ, (2010) Mitochondrial membrane potential regulates PINK1 import and proteolytic destabilization by PARL. J Cell Biol 191: 933-942
    • (2010) J Cell Biol , vol.191 , pp. 933-942
    • Jin, S.M.1    Lazarou, M.2    Wang, C.3    Kane, L.A.4    Narendra, D.P.5    Youle, R.J.6
  • 102
    • 79955667485 scopus 로고    scopus 로고
    • The mitochondrial intramembrane protease PARL cleaves human Pink1 to regulate Pink1 trafficking
    • Meissner C, Lorenz H, Weihofen A, Selkoe DJ, Lemberg MK, (2011) The mitochondrial intramembrane protease PARL cleaves human Pink1 to regulate Pink1 trafficking. J Neurochem 117: 856-867
    • (2011) J Neurochem , vol.117 , pp. 856-867
    • Meissner, C.1    Lorenz, H.2    Weihofen, A.3    Selkoe, D.J.4    Lemberg, M.K.5
  • 105
    • 84887453820 scopus 로고    scopus 로고
    • PINK1 is degraded through the N-end rule pathway
    • Yamano K, Youle RJ, (2013) PINK1 is degraded through the N-end rule pathway. Autophagy 9: 1758-1769
    • (2013) Autophagy , vol.9 , pp. 1758-1769
    • Yamano, K.1    Youle, R.J.2
  • 107
    • 55249113916 scopus 로고    scopus 로고
    • Step-size analyses of the mitochondrial Hsp70 import motor reveal the Brownian ratchet in operation
    • Yamano K, Kuroyanagi-Hasegawa M, Esaki M, Yokota M, Endo T, (2008) Step-size analyses of the mitochondrial Hsp70 import motor reveal the Brownian ratchet in operation. J Biol Chem 283: 27325-27332
    • (2008) J Biol Chem , vol.283 , pp. 27325-27332
    • Yamano, K.1    Kuroyanagi-Hasegawa, M.2    Esaki, M.3    Yokota, M.4    Endo, T.5
  • 108
    • 0038771224 scopus 로고    scopus 로고
    • Substrate specificity of rhomboid intramembrane proteases is governed by helix-breaking residues in the substrate transmembrane domain
    • Urban S, Freeman M, (2003) Substrate specificity of rhomboid intramembrane proteases is governed by helix-breaking residues in the substrate transmembrane domain. Mol Cell 11: 1425-1434
    • (2003) Mol Cell , vol.11 , pp. 1425-1434
    • Urban, S.1    Freeman, M.2
  • 109
    • 24944483742 scopus 로고    scopus 로고
    • Proline residues of transmembrane domains determine the sorting of inner membrane proteins in mitochondria
    • Meier S, Neupert W, Herrmann JM, (2005) Proline residues of transmembrane domains determine the sorting of inner membrane proteins in mitochondria. J Cell Biol 170: 881-888
    • (2005) J Cell Biol , vol.170 , pp. 881-888
    • Meier, S.1    Neupert, W.2    Herrmann, J.M.3
  • 113
    • 84901615924 scopus 로고    scopus 로고
    • PINK1-Parkin pathway activity is regulated by degradation of PINK1 in the mitochondrial matrix
    • Thomas RE, Andrews LA, Burman JL, Lin WY, Pallanck LJ, (2014) PINK1-Parkin pathway activity is regulated by degradation of PINK1 in the mitochondrial matrix. PLoS Genet 10: e1004279
    • (2014) PLoS Genet , vol.10 , pp. e1004279
    • Thomas, R.E.1    Andrews, L.A.2    Burman, J.L.3    Lin, W.Y.4    Pallanck, L.J.5
  • 114
    • 84866244791 scopus 로고    scopus 로고
    • Autophagy in protein and organelle turnover
    • Mizushima N, (2011) Autophagy in protein and organelle turnover. Cold Spring Harb Symp Quant Biol 76: 397-402
    • (2011) Cold Spring Harb Symp Quant Biol , vol.76 , pp. 397-402
    • Mizushima, N.1
  • 116
    • 84901801108 scopus 로고    scopus 로고
    • Organellophagy: Eliminating cellular building blocks via selective autophagy
    • Okamoto K, (2014) Organellophagy: eliminating cellular building blocks via selective autophagy. J Cell Biol 205: 435-445
    • (2014) J Cell Biol , vol.205 , pp. 435-445
    • Okamoto, K.1
  • 117
    • 84901815187 scopus 로고    scopus 로고
    • Cargo recognition and trafficking in selective autophagy
    • Stolz A, Ernst A, Dikic I, (2014) Cargo recognition and trafficking in selective autophagy. Nat Cell Biol 16: 495-501
    • (2014) Nat Cell Biol , vol.16 , pp. 495-501
    • Stolz, A.1    Ernst, A.2    Dikic, I.3
  • 119
    • 81055144784 scopus 로고    scopus 로고
    • Autophagy: Renovation of cells and tissues
    • Mizushima N, Komatsu M, (2011) Autophagy: renovation of cells and tissues. Cell 147: 728-741
    • (2011) Cell , vol.147 , pp. 728-741
    • Mizushima, N.1    Komatsu, M.2
  • 122
    • 84857850213 scopus 로고    scopus 로고
    • Structures containing Atg9A and the ULK1 complex independently target depolarized mitochondria at initial stages of Parkin-mediated mitophagy
    • Itakura E, Kishi-Itakura C, Koyama-Honda I, Mizushima N, (2012) Structures containing Atg9A and the ULK1 complex independently target depolarized mitochondria at initial stages of Parkin-mediated mitophagy. J Cell Sci 125: 1488-1499
    • (2012) J Cell Sci , vol.125 , pp. 1488-1499
    • Itakura, E.1    Kishi-Itakura, C.2    Koyama-Honda, I.3    Mizushima, N.4
  • 124
    • 64049113909 scopus 로고    scopus 로고
    • Distinct regulation of autophagic activity by Atg14L and Rubicon associated with Beclin 1-phosphatidylinositol-3-kinase complex
    • Zhong Y, Wang QJ, Li X, Yan Y, Backer JM, Chait BT, Heintz N, Yue Z, (2009) Distinct regulation of autophagic activity by Atg14L and Rubicon associated with Beclin 1-phosphatidylinositol-3-kinase complex. Nat Cell Biol 11: 468-476
    • (2009) Nat Cell Biol , vol.11 , pp. 468-476
    • Zhong, Y.1    Wang, Q.J.2    Li, X.3    Yan, Y.4    Backer, J.M.5    Chait, B.T.6    Heintz, N.7    Yue, Z.8
  • 126
    • 50249084987 scopus 로고    scopus 로고
    • Autophagosome formation from membrane compartments enriched in phosphatidylinositol 3-phosphate and dynamically connected to the endoplasmic reticulum
    • Axe EL, Walker SA, Manifava M, Chandra P, Roderick HL, Habermann A, Griffiths G, Ktistakis NT, (2008) Autophagosome formation from membrane compartments enriched in phosphatidylinositol 3-phosphate and dynamically connected to the endoplasmic reticulum. J Cell Biol 182: 685-701
    • (2008) J Cell Biol , vol.182 , pp. 685-701
    • Axe, E.L.1    Walker, S.A.2    Manifava, M.3    Chandra, P.4    Roderick, H.L.5    Habermann, A.6    Griffiths, G.7    Ktistakis, N.T.8
  • 127
    • 84908065760 scopus 로고    scopus 로고
    • Optineurin is an autophagy receptor for damaged mitochondria in parkin-mediated mitophagy that is disrupted by an ALS-linked mutation
    • Wong YC, Holzbaur EL, (2014) Optineurin is an autophagy receptor for damaged mitochondria in parkin-mediated mitophagy that is disrupted by an ALS-linked mutation. Proc Natl Acad Sci USA 111: E4439-E4448
    • (2014) Proc Natl Acad Sci USA , vol.111 , pp. E4439-E4448
    • Wong, Y.C.1    Holzbaur, E.L.2
  • 128
    • 77953122645 scopus 로고    scopus 로고
    • LC3 and GATE-16/GABARAP subfamilies are both essential yet act differently in autophagosome biogenesis
    • Weidberg H, Shvets E, Shpilka T, Shimron F, Shinder V, Elazar Z, (2010) LC3 and GATE-16/GABARAP subfamilies are both essential yet act differently in autophagosome biogenesis. EMBO J 29: 1792-1802
    • (2010) EMBO J , vol.29 , pp. 1792-1802
    • Weidberg, H.1    Shvets, E.2    Shpilka, T.3    Shimron, F.4    Shinder, V.5    Elazar, Z.6
  • 130
    • 78649300971 scopus 로고    scopus 로고
    • P62/SQSTM1 is required for Parkin-induced mitochondrial clustering but not mitophagy; VDAC1 is dispensable for both
    • Narendra D, Kane LA, Hauser DN, Fearnley IM, Youle RJ, (2010) p62/SQSTM1 is required for Parkin-induced mitochondrial clustering but not mitophagy; VDAC1 is dispensable for both. Autophagy 6: 1090-1106
    • (2010) Autophagy , vol.6 , pp. 1090-1106
    • Narendra, D.1    Kane, L.A.2    Hauser, D.N.3    Fearnley, I.M.4    Youle, R.J.5
  • 132
    • 84951930787 scopus 로고    scopus 로고
    • The PINK1-PARKIN mitochondrial ubiquitylation pathway drives a program of OPTN/NDP52 recruitment and TBK1 activation to promote mitophagy
    • Heo JM, Ordureau A, Paulo JA, Rinehart J, Harper JW, (2015) The PINK1-PARKIN mitochondrial ubiquitylation pathway drives a program of OPTN/NDP52 recruitment and TBK1 activation to promote mitophagy. Mol Cell 60: 7-20
    • (2015) Mol Cell , vol.60 , pp. 7-20
    • Heo, J.M.1    Ordureau, A.2    Paulo, J.A.3    Rinehart, J.4    Harper, J.W.5
  • 134
    • 84940753095 scopus 로고    scopus 로고
    • TBK1 controls autophagosomal engulfment of polyubiquitinated mitochondria through p62/SQSTM1 phosphorylation
    • Matsumoto G, Shimogori T, Hattori N, Nukina N, (2015) TBK1 controls autophagosomal engulfment of polyubiquitinated mitochondria through p62/SQSTM1 phosphorylation. Hum Mol Genet 24: 4429-4442
    • (2015) Hum Mol Genet , vol.24 , pp. 4429-4442
    • Matsumoto, G.1    Shimogori, T.2    Hattori, N.3    Nukina, N.4
  • 135
    • 80053917869 scopus 로고    scopus 로고
    • Polyubiquitin binding to optineurin is required for optimal activation of TANK-binding kinase 1 and production of interferon beta
    • Gleason CE, Ordureau A, Gourlay R, Arthur JS, Cohen P, (2011) Polyubiquitin binding to optineurin is required for optimal activation of TANK-binding kinase 1 and production of interferon beta. J Biol Chem 286: 35663-35674
    • (2011) J Biol Chem , vol.286 , pp. 35663-35674
    • Gleason, C.E.1    Ordureau, A.2    Gourlay, R.3    Arthur, J.S.4    Cohen, P.5
  • 136
    • 84898624312 scopus 로고    scopus 로고
    • Self and nonself: How autophagy targets mitochondria and bacteria
    • Randow F, Youle RJ, (2014) Self and nonself: how autophagy targets mitochondria and bacteria. Cell Host Microbe 15: 403-411
    • (2014) Cell Host Microbe , vol.15 , pp. 403-411
    • Randow, F.1    Youle, R.J.2
  • 138
    • 84898652320 scopus 로고    scopus 로고
    • Mitochondrial Rab GAPs govern autophagosome biogenesis during mitophagy
    • Yamano K, Fogel AI, Wang C, van der Bliek AM, Youle RJ, (2014) Mitochondrial Rab GAPs govern autophagosome biogenesis during mitophagy. eLife 3: e01612
    • (2014) ELife , vol.3 , pp. e01612
    • Yamano, K.1    Fogel, A.I.2    Wang, C.3    Van Der Bliek, A.M.4    Youle, R.J.5
  • 139
    • 73549102459 scopus 로고    scopus 로고
    • An initial step of GAS-containing autophagosome-like vacuoles formation requires Rab7
    • Yamaguchi H, Nakagawa I, Yamamoto A, Amano A, Noda T, Yoshimori T, (2009) An initial step of GAS-containing autophagosome-like vacuoles formation requires Rab7. PLoS Pathog 5: e1000670
    • (2009) PLoS Pathog , vol.5 , pp. e1000670
    • Yamaguchi, H.1    Nakagawa, I.2    Yamamoto, A.3    Amano, A.4    Noda, T.5    Yoshimori, T.6
  • 142
    • 80052716148 scopus 로고    scopus 로고
    • Characterization of the CLEAR network reveals an integrated control of cellular clearance pathways
    • Palmieri M, Impey S, Kang H, di Ronza A, Pelz C, Sardiello M, Ballabio A, (2011) Characterization of the CLEAR network reveals an integrated control of cellular clearance pathways. Hum Mol Genet 20: 3852-3866
    • (2011) Hum Mol Genet , vol.20 , pp. 3852-3866
    • Palmieri, M.1    Impey, S.2    Kang, H.3    Di Ronza, A.4    Pelz, C.5    Sardiello, M.6    Ballabio, A.7
  • 143
    • 84874352229 scopus 로고    scopus 로고
    • Rag GTPases mediate amino acid-dependent recruitment of TFEB and MITF to lysosomes
    • Martina JA, Puertollano R, (2013) Rag GTPases mediate amino acid-dependent recruitment of TFEB and MITF to lysosomes. J Cell Biol 200: 475-491
    • (2013) J Cell Biol , vol.200 , pp. 475-491
    • Martina, J.A.1    Puertollano, R.2
  • 145
    • 84864874958 scopus 로고    scopus 로고
    • MTORC1 functions as a transcriptional regulator of autophagy by preventing nuclear transport of TFEB
    • Martina JA, Chen Y, Gucek M, Puertollano R, (2012) MTORC1 functions as a transcriptional regulator of autophagy by preventing nuclear transport of TFEB. Autophagy 8: 903-914
    • (2012) Autophagy , vol.8 , pp. 903-914
    • Martina, J.A.1    Chen, Y.2    Gucek, M.3    Puertollano, R.4
  • 147
    • 84939820927 scopus 로고    scopus 로고
    • MiT/TFE transcription factors are activated during mitophagy downstream of Parkin and Atg5
    • Nezich CL, Wang C, Fogel AI, Youle RJ, (2015) MiT/TFE transcription factors are activated during mitophagy downstream of Parkin and Atg5. J Cell Biol 210: 435-450
    • (2015) J Cell Biol , vol.210 , pp. 435-450
    • Nezich, C.L.1    Wang, C.2    Fogel, A.I.3    Youle, R.J.4
  • 152
    • 84897863239 scopus 로고    scopus 로고
    • Parkin and PINK1 function in a vesicular trafficking pathway regulating mitochondrial quality control
    • McLelland GL, Soubannier V, Chen CX, McBride HM, Fon EA, (2014) Parkin and PINK1 function in a vesicular trafficking pathway regulating mitochondrial quality control. EMBO J 33: 282-295
    • (2014) EMBO J , vol.33 , pp. 282-295
    • McLelland, G.L.1    Soubannier, V.2    Chen, C.X.3    McBride, H.M.4    Fon, E.A.5
  • 153
    • 84908085343 scopus 로고    scopus 로고
    • A new pathway for mitochondrial quality control: Mitochondrial-derived vesicles
    • Sugiura A, McLelland GL, Fon EA, McBride HM, (2014) A new pathway for mitochondrial quality control: mitochondrial-derived vesicles. EMBO J 33: 2142-2156
    • (2014) EMBO J , vol.33 , pp. 2142-2156
    • Sugiura, A.1    McLelland, G.L.2    Fon, E.A.3    McBride, H.M.4
  • 155
    • 84858701257 scopus 로고    scopus 로고
    • Spatial parkin translocation and degradation of damaged mitochondria via mitophagy in live cortical neurons
    • Cai Q, Zakaria HM, Simone A, Sheng ZH, (2012) Spatial parkin translocation and degradation of damaged mitochondria via mitophagy in live cortical neurons. Curr Biol 22: 545-552
    • (2012) Curr Biol , vol.22 , pp. 545-552
    • Cai, Q.1    Zakaria, H.M.2    Simone, A.3    Sheng, Z.H.4
  • 156
    • 84906861963 scopus 로고    scopus 로고
    • Mitophagy of damaged mitochondria occurs locally in distal neuronal axons and requires PINK1 and Parkin
    • Ashrafi G, Schlehe JS, LaVoie MJ, Schwarz TL, (2014) Mitophagy of damaged mitochondria occurs locally in distal neuronal axons and requires PINK1 and Parkin. J Cell Biol 206: 655-670
    • (2014) J Cell Biol , vol.206 , pp. 655-670
    • Ashrafi, G.1    Schlehe, J.S.2    LaVoie, M.J.3    Schwarz, T.L.4
  • 158
    • 84875234201 scopus 로고    scopus 로고
    • CCCP-induced LC3 lipidation depends on Atg9 whereas FIP200/Atg13 and Beclin 1/Atg14 are dispensable
    • Chen D, Chen X, Li M, Zhang H, Ding WX, Yin XM, (2013) CCCP-induced LC3 lipidation depends on Atg9 whereas FIP200/Atg13 and Beclin 1/Atg14 are dispensable. Biochem Biophys Res Commun 432: 226-230
    • (2013) Biochem Biophys Res Commun , vol.432 , pp. 226-230
    • Chen, D.1    Chen, X.2    Li, M.3    Zhang, H.4    Ding, W.X.5    Yin, X.M.6
  • 159
    • 84887466109 scopus 로고    scopus 로고
    • The protonophore CCCP interferes with lysosomal degradation of autophagic cargo in yeast and mammalian cells
    • Padman BS, Bach M, Lucarelli G, Prescott M, Ramm G, (2013) The protonophore CCCP interferes with lysosomal degradation of autophagic cargo in yeast and mammalian cells. Autophagy 9: 1862-1875
    • (2013) Autophagy , vol.9 , pp. 1862-1875
    • Padman, B.S.1    Bach, M.2    Lucarelli, G.3    Prescott, M.4    Ramm, G.5
  • 160
    • 0024597977 scopus 로고
    • The glycoprotein of VSV accumulates in a distal Golgi compartment in the presence of CCCP
    • Burkhardt JK, Hester S, Argon Y, (1989) The glycoprotein of VSV accumulates in a distal Golgi compartment in the presence of CCCP. J Cell Sci 92 (Pt 4): 643-654
    • (1989) J Cell Sci , vol.92 , pp. 643-654
    • Burkhardt, J.K.1    Hester, S.2    Argon, Y.3
  • 161
    • 0032499784 scopus 로고    scopus 로고
    • Measurement of cytosolic, mitochondrial, and Golgi pH in single living cells with green fluorescent proteins
    • Llopis J, McCaffery JM, Miyawaki A, Farquhar MG, Tsien RY, (1998) Measurement of cytosolic, mitochondrial, and Golgi pH in single living cells with green fluorescent proteins. Proc Natl Acad Sci USA 95: 6803-6808
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 6803-6808
    • Llopis, J.1    McCaffery, J.M.2    Miyawaki, A.3    Farquhar, M.G.4    Tsien, R.Y.5
  • 163
    • 77950384477 scopus 로고    scopus 로고
    • Drosophila parkin requires PINK1 for mitochondrial translocation and ubiquitinates mitofusin
    • Ziviani E, Tao RN, Whitworth AJ, (2010) Drosophila parkin requires PINK1 for mitochondrial translocation and ubiquitinates mitofusin. Proc Natl Acad Sci USA 107: 5018-5023
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 5018-5023
    • Ziviani, E.1    Tao, R.N.2    Whitworth, A.J.3
  • 164
    • 0027104639 scopus 로고
    • Relation of superoxide generation and lipid peroxidation to the inhibition of NADH-Q oxidoreductase by rotenone, piericidin A, and MPP+
    • Ramsay RR, Singer TP, (1992) Relation of superoxide generation and lipid peroxidation to the inhibition of NADH-Q oxidoreductase by rotenone, piericidin A, and MPP+. Biochem Biophys Res Commun 189: 47-52
    • (1992) Biochem Biophys Res Commun , vol.189 , pp. 47-52
    • Ramsay, R.R.1    Singer, T.P.2
  • 167
    • 84867273800 scopus 로고    scopus 로고
    • ROS-induced mitochondrial depolarization initiates PARK2/PARKIN-dependent mitochondrial degradation by autophagy
    • Wang Y, Nartiss Y, Steipe B, McQuibban GA, Kim PK, (2012) ROS-induced mitochondrial depolarization initiates PARK2/PARKIN-dependent mitochondrial degradation by autophagy. Autophagy 8: 1462-1476
    • (2012) Autophagy , vol.8 , pp. 1462-1476
    • Wang, Y.1    Nartiss, Y.2    Steipe, B.3    McQuibban, G.A.4    Kim, P.K.5
  • 168
    • 80053430054 scopus 로고    scopus 로고
    • Spatiotemporally controlled initiation of Parkin-mediated mitophagy within single cells
    • Yang JY, Yang WY, (2011) Spatiotemporally controlled initiation of Parkin-mediated mitophagy within single cells. Autophagy 7: 1230-1238
    • (2011) Autophagy , vol.7 , pp. 1230-1238
    • Yang, J.Y.1    Yang, W.Y.2
  • 171
    • 84887486172 scopus 로고    scopus 로고
    • The accumulation of misfolded proteins in the mitochondrial matrix is sensed by PINK1 to induce PARK2/Parkin-mediated mitophagy of polarized mitochondria
    • Jin SM, Youle RJ, (2013) The accumulation of misfolded proteins in the mitochondrial matrix is sensed by PINK1 to induce PARK2/Parkin-mediated mitophagy of polarized mitochondria. Autophagy 9: 1750-1757
    • (2013) Autophagy , vol.9 , pp. 1750-1757
    • Jin, S.M.1    Youle, R.J.2
  • 172
    • 80052145606 scopus 로고    scopus 로고
    • A sensitive and quantitative technique for detecting autophagic events based on lysosomal delivery
    • Katayama H, Kogure T, Mizushima N, Yoshimori T, Miyawaki A, (2011) A sensitive and quantitative technique for detecting autophagic events based on lysosomal delivery. Chem Biol 18: 1042-1052
    • (2011) Chem Biol , vol.18 , pp. 1042-1052
    • Katayama, H.1    Kogure, T.2    Mizushima, N.3    Yoshimori, T.4    Miyawaki, A.5
  • 178
    • 79960716413 scopus 로고    scopus 로고
    • Regulating mitochondrial outer membrane proteins by ubiquitination and proteasomal degradation
    • Karbowski M, Youle RJ, (2011) Regulating mitochondrial outer membrane proteins by ubiquitination and proteasomal degradation. Curr Opin Cell Biol 23: 476-482
    • (2011) Curr Opin Cell Biol , vol.23 , pp. 476-482
    • Karbowski, M.1    Youle, R.J.2


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