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Volumn 31, Issue 2, 2016, Pages 178-192

Autophagy and Alpha-Synuclein: Relevance to Parkinson's Disease and Related Synucleopathies

Author keywords

alpha synuclein; chaperone mediated autophagy; glucocerebrosidase; lysosomes; macroautophagy; neurodegeneration; Parkinson's disease; synucleinopathies

Indexed keywords

ALPHA SYNUCLEIN; GLUCOSYLCERAMIDASE;

EID: 84958020018     PISSN: 08853185     EISSN: 15318257     Source Type: Journal    
DOI: 10.1002/mds.26477     Document Type: Review
Times cited : (225)

References (147)
  • 3
    • 84879606955 scopus 로고    scopus 로고
    • Alpha-synuclein and protein degradation systems: a reciprocal relationship
    • Xilouri M, Brekk OR, Stefanis L. Alpha-synuclein and protein degradation systems: a reciprocal relationship. Mol Neurobiol 2013;47:537–551.
    • (2013) Mol Neurobiol , vol.47 , pp. 537-551
    • Xilouri, M.1    Brekk, O.R.2    Stefanis, L.3
  • 4
    • 84883420073 scopus 로고    scopus 로고
    • Dysfunction of the autophagy/lysosomal degradation pathway is a shared feature of the genetic synucleinopathies
    • Manzoni C, Lewis PA. Dysfunction of the autophagy/lysosomal degradation pathway is a shared feature of the genetic synucleinopathies. FASEB J 2013;27:3424–3429.
    • (2013) FASEB J , vol.27 , pp. 3424-3429
    • Manzoni, C.1    Lewis, P.A.2
  • 5
    • 69249106881 scopus 로고    scopus 로고
    • Pathways and mechanisms of endocytic recycling
    • Grant BD, Donaldson JG. Pathways and mechanisms of endocytic recycling. Nat Rev Mol Cell Biol 2009;10:597–608.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 597-608
    • Grant, B.D.1    Donaldson, J.G.2
  • 6
    • 0034735536 scopus 로고    scopus 로고
    • Autophagic tubes: vacuolar invaginations involved in lateral membrane sorting and inverse vesicle budding
    • Muller O, Sattler T, Flotenmeyer M, Schwarz H, Plattner H, Mayer A. Autophagic tubes: vacuolar invaginations involved in lateral membrane sorting and inverse vesicle budding. J Cell Biol 2000;151:519–528.
    • (2000) J Cell Biol , vol.151 , pp. 519-528
    • Muller, O.1    Sattler, T.2    Flotenmeyer, M.3    Schwarz, H.4    Plattner, H.5    Mayer, A.6
  • 7
    • 79551598347 scopus 로고    scopus 로고
    • AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1
    • Kim J, Kundu M, Viollet B, Guan KL. AMPK and mTOR regulate autophagy through direct phosphorylation of Ulk1. Nat Cell Biol 2011;13:132–141.
    • (2011) Nat Cell Biol , vol.13 , pp. 132-141
    • Kim, J.1    Kundu, M.2    Viollet, B.3    Guan, K.L.4
  • 8
    • 77951214016 scopus 로고    scopus 로고
    • Mammalian autophagy: core molecular machinery and signaling regulation
    • Yang Z, Klionsky DJ. Mammalian autophagy: core molecular machinery and signaling regulation. Curr Opin Cell Biol 2010;22:124–131.
    • (2010) Curr Opin Cell Biol , vol.22 , pp. 124-131
    • Yang, Z.1    Klionsky, D.J.2
  • 10
    • 79957663035 scopus 로고    scopus 로고
    • Lysosomal proteolysis inhibition selectively disrupts axonal transport of degradative organelles and causes an Alzheimer's-like axonal dystrophy
    • Lee S, Sato Y, Nixon RA. Lysosomal proteolysis inhibition selectively disrupts axonal transport of degradative organelles and causes an Alzheimer's-like axonal dystrophy. J Neurosci 2011;31:7817–7830.
    • (2011) J Neurosci , vol.31 , pp. 7817-7830
    • Lee, S.1    Sato, Y.2    Nixon, R.A.3
  • 11
    • 84904266112 scopus 로고    scopus 로고
    • Autophagosome biogenesis in primary neurons follows an ordered and spatially regulated pathway
    • Maday S, Holzbaur EL. Autophagosome biogenesis in primary neurons follows an ordered and spatially regulated pathway. Dev Cell 2014;30:71–85.
    • (2014) Dev Cell , vol.30 , pp. 71-85
    • Maday, S.1    Holzbaur, E.L.2
  • 13
    • 84901815187 scopus 로고    scopus 로고
    • Cargo recognition and trafficking in selective autophagy
    • Stolz A, Ernst A, Dikic I. Cargo recognition and trafficking in selective autophagy. Nat Cell Biol 2014;16:495–501.
    • (2014) Nat Cell Biol , vol.16 , pp. 495-501
    • Stolz, A.1    Ernst, A.2    Dikic, I.3
  • 14
    • 70350450808 scopus 로고    scopus 로고
    • The TBK1 adaptor and autophagy receptor NDP52 restricts the proliferation of ubiquitin-coated bacteria
    • Thurston TL, Ryzhakov G, Bloor S, von Muhlinen N, Randow F. The TBK1 adaptor and autophagy receptor NDP52 restricts the proliferation of ubiquitin-coated bacteria. Nat Immunol 2009;10:1215–1221.
    • (2009) Nat Immunol , vol.10 , pp. 1215-1221
    • Thurston, T.L.1    Ryzhakov, G.2    Bloor, S.3    von Muhlinen, N.4    Randow, F.5
  • 15
    • 74049153002 scopus 로고    scopus 로고
    • Nix is a selective autophagy receptor for mitochondrial clearance
    • Novak I, Kirkin V, McEwan DG, et al. Nix is a selective autophagy receptor for mitochondrial clearance. EMBO Rep 2009;11:45–51.
    • (2009) EMBO Rep , vol.11 , pp. 45-51
    • Novak, I.1    Kirkin, V.2    McEwan, D.G.3
  • 16
    • 67650264633 scopus 로고    scopus 로고
    • Atg32 is a mitochondrial protein that confers selectivity during mitophagy
    • Kanki T, Wang K, Cao Y, Baba M, Klionsky DJ. Atg32 is a mitochondrial protein that confers selectivity during mitophagy. Dev Cell 2009;17:98–109.
    • (2009) Dev Cell , vol.17 , pp. 98-109
    • Kanki, T.1    Wang, K.2    Cao, Y.3    Baba, M.4    Klionsky, D.J.5
  • 17
    • 60849099049 scopus 로고    scopus 로고
    • A role for NBR1 in autophagosomal degradation of ubiquitinated substrates
    • Kirkin V, Lamark T, Sou YS, et al. A role for NBR1 in autophagosomal degradation of ubiquitinated substrates. Mol Cell 2009;33:505–516.
    • (2009) Mol Cell , vol.33 , pp. 505-516
    • Kirkin, V.1    Lamark, T.2    Sou, Y.S.3
  • 18
    • 84883451249 scopus 로고    scopus 로고
    • Selective autophagy: talking with the UPS
    • Park C, Cuervo AM. Selective autophagy: talking with the UPS. Cell Biochem Biophys 2013;67:3–13.
    • (2013) Cell Biochem Biophys , vol.67 , pp. 3-13
    • Park, C.1    Cuervo, A.M.2
  • 19
    • 0025294506 scopus 로고
    • Peptide sequences that target cytosolic proteins for lysosomal proteolysis
    • Dice JF. Peptide sequences that target cytosolic proteins for lysosomal proteolysis. Trends Biochem Sci 1990;15:305–309.
    • (1990) Trends Biochem Sci , vol.15 , pp. 305-309
    • Dice, J.F.1
  • 20
    • 0023891846 scopus 로고
    • Peptide sequences that target proteins for enhanced degradation during serum withdrawal
    • Chiang HL, Dice JF. Peptide sequences that target proteins for enhanced degradation during serum withdrawal. J Biol Chem 1988;263:6797–6805.
    • (1988) J Biol Chem , vol.263 , pp. 6797-6805
    • Chiang, H.L.1    Dice, J.F.2
  • 21
    • 0034914206 scopus 로고    scopus 로고
    • A molecular chaperone complex at the lysosomal membrane is required for protein translocation
    • Agarraberes FA, Dice JF. A molecular chaperone complex at the lysosomal membrane is required for protein translocation. J Cell Sci 2001;114(Pt 13):2491–2499.
    • (2001) J Cell Sci , vol.114 , pp. 2491-2499
    • Agarraberes, F.A.1    Dice, J.F.2
  • 22
    • 0029837453 scopus 로고    scopus 로고
    • A receptor for the selective uptake and degradation of proteins by lysosomes
    • Cuervo AM, Dice JF. A receptor for the selective uptake and degradation of proteins by lysosomes. Science 1996;273:501–503.
    • (1996) Science , vol.273 , pp. 501-503
    • Cuervo, A.M.1    Dice, J.F.2
  • 23
    • 51349130544 scopus 로고    scopus 로고
    • The chaperone-mediated autophagy receptor organizes in dynamic protein complexes at the lysosomal membrane
    • Bandyopadhyay U, Kaushik S, Varticovski L, Cuervo AM. The chaperone-mediated autophagy receptor organizes in dynamic protein complexes at the lysosomal membrane. Mol Cell Biol 2008;28:5747–5763.
    • (2008) Mol Cell Biol , vol.28 , pp. 5747-5763
    • Bandyopadhyay, U.1    Kaushik, S.2    Varticovski, L.3    Cuervo, A.M.4
  • 25
    • 0034232418 scopus 로고    scopus 로고
    • Regulation of Lamp2a levels in the lysosomal membrane
    • Cuervo AM, Dice JF. Regulation of Lamp2a levels in the lysosomal membrane. Traffic 2000;1:570–583.
    • (2000) Traffic , vol.1 , pp. 570-583
    • Cuervo, A.M.1    Dice, J.F.2
  • 26
    • 0028848119 scopus 로고
    • Activation of a selective pathway of lysosomal proteolysis in rat liver by prolonged starvation
    • Cuervo AM, Knecht E, Terlecky SR, Dice JF. Activation of a selective pathway of lysosomal proteolysis in rat liver by prolonged starvation. Am J Physiol 1995;269(5 Pt 1):C1200–C1208.
    • (1995) Am J Physiol , vol.269 , Issue.5 , pp. C1200-C1208
    • Cuervo, A.M.1    Knecht, E.2    Terlecky, S.R.3    Dice, J.F.4
  • 27
    • 0030923854 scopus 로고    scopus 로고
    • An intralysosomal hsp70 is required for a selective pathway of lysosomal protein degradation
    • Agarraberes FA, Terlecky SR, Dice JF. An intralysosomal hsp70 is required for a selective pathway of lysosomal protein degradation. J Cell Biol 1997;137:825–834.
    • (1997) J Cell Biol , vol.137 , pp. 825-834
    • Agarraberes, F.A.1    Terlecky, S.R.2    Dice, J.F.3
  • 28
    • 84937520970 scopus 로고    scopus 로고
    • Lysosomal mTORC2/PHLPP1/Akt regulate chaperone-mediated autophagy
    • Arias E, Koga H, Diaz A, Mocholi E, Patel B, Cuervo AM. Lysosomal mTORC2/PHLPP1/Akt regulate chaperone-mediated autophagy. Mol Cell 2015;59:270–284.
    • (2015) Mol Cell , vol.59 , pp. 270-284
    • Arias, E.1    Koga, H.2    Diaz, A.3    Mocholi, E.4    Patel, B.5    Cuervo, A.M.6
  • 29
    • 84878775231 scopus 로고    scopus 로고
    • Lipofuscin: formation, effects and role of macroautophagy
    • Hohn A, Grune T. Lipofuscin: formation, effects and role of macroautophagy. Redox Biol 2013;1:140–144.
    • (2013) Redox Biol , vol.1 , pp. 140-144
    • Hohn, A.1    Grune, T.2
  • 30
    • 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. alpha-Synuclein in filamentous inclusions of Lewy bodies from Parkinson's disease and dementia with Lewy bodies. Proc Natl Acad Sci U S A 1998;95:6469–6473.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 6469-6473
    • Spillantini, M.G.1    Crowther, R.A.2    Jakes, R.3    Hasegawa, M.4    Goedert, M.5
  • 32
    • 4644290985 scopus 로고    scopus 로고
    • Alpha-synuclein locus duplication as a cause of familial Parkinson's disease
    • Chartier-Harlin MC, Kachergus J, Roumier C, et al. Alpha-synuclein locus duplication as a cause of familial Parkinson's disease. Lancet 2004;364:1167–1169.
    • (2004) Lancet , vol.364 , pp. 1167-1169
    • Chartier-Harlin, M.C.1    Kachergus, J.2    Roumier, C.3
  • 33
    • 0030744876 scopus 로고    scopus 로고
    • Mutation in the alpha-synuclein gene identified in families with Parkinson's disease
    • Polymeropoulos MH, Lavedan C, Leroy E, et al. Mutation in the alpha-synuclein gene identified in families with Parkinson's disease. Science 1997;276:2045–2047.
    • (1997) Science , vol.276 , pp. 2045-2047
    • Polymeropoulos, M.H.1    Lavedan, C.2    Leroy, E.3
  • 34
    • 0031990490 scopus 로고    scopus 로고
    • Ala30Pro mutation in the gene encoding alpha-synuclein in Parkinson's disease
    • Kruger R, Kuhn W, Muller T, et al. Ala30Pro mutation in the gene encoding alpha-synuclein in Parkinson's disease. Nat Genet 1998;18:106–108.
    • (1998) Nat Genet , vol.18 , pp. 106-108
    • Kruger, R.1    Kuhn, W.2    Muller, T.3
  • 35
    • 0242300619 scopus 로고    scopus 로고
    • alpha-Synuclein locus triplication causes Parkinson's disease
    • Singleton AB, Singleton A, Hague S, et al. alpha-Synuclein locus triplication causes Parkinson's disease. Science 2003;302:841.
    • (2003) Science , vol.302 , pp. 841
    • Singleton, A.B.1    Singleton, A.2    Hague, S.3
  • 36
    • 33746869343 scopus 로고    scopus 로고
    • Collaborative analysis of alpha-synuclein gene promoter variability and Parkinson disease
    • Maraganore DM, de Andrade M, Elbaz A, et al. Collaborative analysis of alpha-synuclein gene promoter variability and Parkinson disease. JAMA 2006;296:661–670.
    • (2006) JAMA , vol.296 , pp. 661-670
    • Maraganore, D.M.1    de Andrade, M.2    Elbaz, A.3
  • 37
    • 69149089036 scopus 로고    scopus 로고
    • Molecular pathogenesis of Parkinson disease: insights from genetic studies
    • Gasser T. Molecular pathogenesis of Parkinson disease: insights from genetic studies. Exp Rev Mol Med 2009;11:e22.
    • (2009) Exp Rev Mol Med , vol.11
    • Gasser, T.1
  • 38
    • 70549088602 scopus 로고    scopus 로고
    • Genome-wide association study reveals genetic risk underlying Parkinson's disease
    • Simon-Sanchez J, Schulte C, Bras JM, et al. Genome-wide association study reveals genetic risk underlying Parkinson's disease. Nat Genet 2009;41:1308–1312.
    • (2009) Nat Genet , vol.41 , pp. 1308-1312
    • Simon-Sanchez, J.1    Schulte, C.2    Bras, J.M.3
  • 40
    • 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. Parkin suppresses unfolded protein stress-induced cell death through its E3 ubiquitin-protein ligase activity. J Biol Chem 2000;275:35661–35664.
    • (2000) J Biol Chem , vol.275 , pp. 35661-35664
    • Imai, Y.1    Soda, M.2    Takahashi, R.3
  • 42
    • 1442275729 scopus 로고    scopus 로고
    • Clearance of alpha-synuclein oligomeric intermediates via the lysosomal degradation pathway
    • Lee HJ, Khoshaghideh F, Patel S, Lee SJ. Clearance of alpha-synuclein oligomeric intermediates via the lysosomal degradation pathway. J Neurosci 2004;24:1888–1896.
    • (2004) J Neurosci , vol.24 , pp. 1888-1896
    • Lee, H.J.1    Khoshaghideh, F.2    Patel, S.3    Lee, S.J.4
  • 43
    • 4344659685 scopus 로고    scopus 로고
    • Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy
    • Cuervo AM, Stefanis L, Fredenburg R, Lansbury PT, Sulzer D. Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy. Science 2004;305:1292–1295.
    • (2004) Science , vol.305 , pp. 1292-1295
    • Cuervo, A.M.1    Stefanis, L.2    Fredenburg, R.3    Lansbury, P.T.4    Sulzer, D.5
  • 44
    • 53049098471 scopus 로고    scopus 로고
    • Wild type alpha-synuclein is degraded by chaperone-mediated autophagy and macroautophagy in neuronal cells
    • Vogiatzi T, Xilouri M, Vekrellis K, Stefanis L. Wild type alpha-synuclein is degraded by chaperone-mediated autophagy and macroautophagy in neuronal cells. J Biol Chem 2008;283:23542–23556.
    • (2008) J Biol Chem , vol.283 , pp. 23542-23556
    • Vogiatzi, T.1    Xilouri, M.2    Vekrellis, K.3    Stefanis, L.4
  • 45
    • 84862598619 scopus 로고    scopus 로고
    • Alpha-synuclein aggregation involves a bafilomycin A 1-sensitive autophagy pathway
    • Klucken J, Poehler AM, Ebrahimi-Fakhari D, et al. Alpha-synuclein aggregation involves a bafilomycin A 1-sensitive autophagy pathway. Autophagy 2012;8:754–766.
    • (2012) Autophagy , vol.8 , pp. 754-766
    • Klucken, J.1    Poehler, A.M.2    Ebrahimi-Fakhari, D.3
  • 46
    • 68449089023 scopus 로고    scopus 로고
    • Metabolic activity determines efficacy of macroautophagic clearance of pathological oligomeric alpha-synuclein
    • Yu WH, Dorado B, Figueroa HY, et al. Metabolic activity determines efficacy of macroautophagic clearance of pathological oligomeric alpha-synuclein. Am J Pathol 2009;175:736–747.
    • (2009) Am J Pathol , vol.175 , pp. 736-747
    • Yu, W.H.1    Dorado, B.2    Figueroa, H.Y.3
  • 47
    • 84869041395 scopus 로고    scopus 로고
    • Development and characterization of a new Parkinson's disease model resulting from impaired autophagy
    • Ahmed I, Liang Y, Schools S, Dawson VL, Dawson TM, Savitt JM. Development and characterization of a new Parkinson's disease model resulting from impaired autophagy. J Neurosci 2012;32:16503–16509.
    • (2012) J Neurosci , vol.32 , pp. 16503-16509
    • Ahmed, I.1    Liang, Y.2    Schools, S.3    Dawson, V.L.4    Dawson, T.M.5    Savitt, J.M.6
  • 48
    • 84861595545 scopus 로고    scopus 로고
    • Disrupted autophagy leads to dopaminergic axon and dendrite degeneration and promotes presynaptic accumulation of alpha-synuclein and LRRK2 in the brain
    • Friedman LG, Lachenmayer ML, Wang J, et al. Disrupted autophagy leads to dopaminergic axon and dendrite degeneration and promotes presynaptic accumulation of alpha-synuclein and LRRK2 in the brain. J Neurosci 2012;32:7585–7593.
    • (2012) J Neurosci , vol.32 , pp. 7585-7593
    • Friedman, L.G.1    Lachenmayer, M.L.2    Wang, J.3
  • 49
    • 80051534540 scopus 로고    scopus 로고
    • A mutation in VPS35, encoding a subunit of the retromer complex, causes late-onset Parkinson disease
    • Zimprich A, Benet-Pages A, Struhal W, et al. A mutation in VPS35, encoding a subunit of the retromer complex, causes late-onset Parkinson disease. Am J Hum Genet 2011;89:168–175.
    • (2011) Am J Hum Genet , vol.89 , pp. 168-175
    • Zimprich, A.1    Benet-Pages, A.2    Struhal, W.3
  • 50
    • 84900460616 scopus 로고    scopus 로고
    • Mutation in VPS35 associated with Parkinson's disease impairs WASH complex association and inhibits autophagy
    • Zavodszky E, Seaman MN, Moreau K, et al. Mutation in VPS35 associated with Parkinson's disease impairs WASH complex association and inhibits autophagy. Nat Commun 2014;5:3828.
    • (2014) Nat Commun , vol.5 , pp. 3828
    • Zavodszky, E.1    Seaman, M.N.2    Moreau, K.3
  • 51
    • 84906503242 scopus 로고    scopus 로고
    • VPS35 dysfunction impairs lysosomal degradation of alpha-synuclein and exacerbates neurotoxicity in a Drosophila model of Parkinson's disease
    • Miura E, Hasegawa T, Konno M, et al. VPS35 dysfunction impairs lysosomal degradation of alpha-synuclein and exacerbates neurotoxicity in a Drosophila model of Parkinson's disease. Neurobiol Dis 2014;71:1–13.
    • (2014) Neurobiol Dis , vol.71 , pp. 1-13
    • Miura, E.1    Hasegawa, T.2    Konno, M.3
  • 52
    • 84920740324 scopus 로고    scopus 로고
    • Parkinson's disease genes VPS35 and EIF4G1 interact genetically and converge on alpha-synuclein
    • Dhungel N, Eleuteri S, Li LB, et al. Parkinson's disease genes VPS35 and EIF4G1 interact genetically and converge on alpha-synuclein. Neuron 2015;85:76–87.
    • (2015) Neuron , vol.85 , pp. 76-87
    • Dhungel, N.1    Eleuteri, S.2    Li, L.B.3
  • 53
    • 33749133430 scopus 로고    scopus 로고
    • Hereditary parkinsonism with dementia is caused by mutations in ATP13A2, encoding a lysosomal type 5 P-type ATPase
    • Ramirez A, Heimbach A, Grundemann J, et al. Hereditary parkinsonism with dementia is caused by mutations in ATP13A2, encoding a lysosomal type 5 P-type ATPase. Nat Genet 2006;38:1184–1191.
    • (2006) Nat Genet , vol.38 , pp. 1184-1191
    • Ramirez, A.1    Heimbach, A.2    Grundemann, J.3
  • 54
    • 84929654352 scopus 로고    scopus 로고
    • The role of ATP13A2 in Parkinson's disease: Clinical phenotypes and molecular mechanisms
    • Park JS, Blair NF, Sue CM. The role of ATP13A2 in Parkinson's disease: Clinical phenotypes and molecular mechanisms. Mov Disord 2015;30:770–779.
    • (2015) Mov Disord , vol.30 , pp. 770-779
    • Park, J.S.1    Blair, N.F.2    Sue, C.M.3
  • 55
    • 84929353414 scopus 로고    scopus 로고
    • alpha-Synuclein-independent histopathological and motor deficits in mice lacking the endolysosomal parkinsonism protein Atp13a2
    • Kett LR, Stiller B, Bernath MM, et al. alpha-Synuclein-independent histopathological and motor deficits in mice lacking the endolysosomal parkinsonism protein Atp13a2. J Neurosci 2015;35:5724–5742.
    • (2015) J Neurosci , vol.35 , pp. 5724-5742
    • Kett, L.R.1    Stiller, B.2    Bernath, M.M.3
  • 56
    • 38849174979 scopus 로고    scopus 로고
    • Dopamine-modified alpha-synuclein blocks chaperone-mediated autophagy
    • Martinez-Vicente M, Talloczy Z, Kaushik S, et al. Dopamine-modified alpha-synuclein blocks chaperone-mediated autophagy. J Clin Invest 2008;118:777–788.
    • (2008) J Clin Invest , vol.118 , pp. 777-788
    • Martinez-Vicente, M.1    Talloczy, Z.2    Kaushik, S.3
  • 58
    • 84885363886 scopus 로고    scopus 로고
    • Polo-like kinase 2 regulates selective autophagic alpha-synuclein clearance and suppresses its toxicity in vivo
    • Oueslati A, Schneider BL, Aebischer P, Lashuel HA. Polo-like kinase 2 regulates selective autophagic alpha-synuclein clearance and suppresses its toxicity in vivo. Proc Natl Acad Sci U S A 2013;110:E3945–E3954.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. E3945-E3954
    • Oueslati, A.1    Schneider, B.L.2    Aebischer, P.3    Lashuel, H.A.4
  • 59
    • 84901361843 scopus 로고    scopus 로고
    • Phosphorylation modulates clearance of alpha-synuclein inclusions in a yeast model of Parkinson's disease
    • Tenreiro S, Reimao-Pinto MM, Antas P, et al. Phosphorylation modulates clearance of alpha-synuclein inclusions in a yeast model of Parkinson's disease. PLoS Genet 2014;10:e1004302.
    • (2014) PLoS Genet , vol.10
    • Tenreiro, S.1    Reimao-Pinto, M.M.2    Antas, P.3
  • 60
    • 84909592222 scopus 로고    scopus 로고
    • Interplay between sumoylation and phosphorylation for protection against alpha-synuclein inclusions
    • Shahpasandzadeh H, Popova B, Kleinknecht A, Fraser PE, Outeiro TF, Braus GH. Interplay between sumoylation and phosphorylation for protection against alpha-synuclein inclusions. J Biol Chem 2014;289:31224–31240.
    • (2014) J Biol Chem , vol.289 , pp. 31224-31240
    • Shahpasandzadeh, H.1    Popova, B.2    Kleinknecht, A.3    Fraser, P.E.4    Outeiro, T.F.5    Braus, G.H.6
  • 62
    • 81755185877 scopus 로고    scopus 로고
    • alpha-Synuclein fate is determined by USP9X-regulated monoubiquitination
    • Rott R, Szargel R, Haskin J, et al. alpha-Synuclein fate is determined by USP9X-regulated monoubiquitination. Proc Natl Acad Sci U S A 2011;108:18666–18671.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 18666-18671
    • Rott, R.1    Szargel, R.2    Haskin, J.3
  • 63
    • 80054026084 scopus 로고    scopus 로고
    • Distinct roles in vivo for the ubiquitin-proteasome system and the autophagy-lysosomal pathway in the degradation of alpha-synuclein
    • Ebrahimi-Fakhari D, Cantuti-Castelvetri I, Fan Z, et al. Distinct roles in vivo for the ubiquitin-proteasome system and the autophagy-lysosomal pathway in the degradation of alpha-synuclein. J Neurosci 2011;31:14508–14520.
    • (2011) J Neurosci , vol.31 , pp. 14508-14520
    • Ebrahimi-Fakhari, D.1    Cantuti-Castelvetri, I.2    Fan, Z.3
  • 64
    • 84859600567 scopus 로고    scopus 로고
    • Targeting intracellular and extracellular alpha-synuclein as a therapeutic strategy in Parkinson's disease and other synucleinopathies
    • Vekrellis K, Stefanis L. Targeting intracellular and extracellular alpha-synuclein as a therapeutic strategy in Parkinson's disease and other synucleinopathies. Exp Opin Ther Targets 2012;16:421–432.
    • (2012) Exp Opin Ther Targets , vol.16 , pp. 421-432
    • Vekrellis, K.1    Stefanis, L.2
  • 65
    • 79954631518 scopus 로고    scopus 로고
    • Lysosomal dysfunction increases exosome-mediated alpha-synuclein release and transmission
    • Alvarez-Erviti L, Seow Y, Schapira AH, et al. Lysosomal dysfunction increases exosome-mediated alpha-synuclein release and transmission. Neurobiol Dis 2011;42:360–367.
    • (2011) Neurobiol Dis , vol.42 , pp. 360-367
    • Alvarez-Erviti, L.1    Seow, Y.2    Schapira, A.H.3
  • 66
    • 84865307818 scopus 로고    scopus 로고
    • Exosomal cell-to-cell transmission of alpha synuclein oligomers
    • Danzer KM, Kranich LR, Ruf WP, et al. Exosomal cell-to-cell transmission of alpha synuclein oligomers. Mol Neurodegener 2012;7:42.
    • (2012) Mol Neurodegener , vol.7 , pp. 42
    • Danzer, K.M.1    Kranich, L.R.2    Ruf, W.P.3
  • 67
    • 84881147729 scopus 로고    scopus 로고
    • Autophagic failure promotes the exocytosis and intercellular transfer of alpha-synuclein
    • Lee HJ, Cho ED, Lee KW, Kim JH, Cho SG, Lee SJ. Autophagic failure promotes the exocytosis and intercellular transfer of alpha-synuclein. Exp Mol Med 2013;45:e22.
    • (2013) Exp Mol Med , vol.45
    • Lee, H.J.1    Cho, E.D.2    Lee, K.W.3    Kim, J.H.4    Cho, S.G.5    Lee, S.J.6
  • 68
    • 84922364789 scopus 로고    scopus 로고
    • Autophagy modulates SNCA/alpha-synuclein release, thereby generating a hostile microenvironment
    • Poehler AM, Xiang W, Spitzer P, et al. Autophagy modulates SNCA/alpha-synuclein release, thereby generating a hostile microenvironment. Autophagy 2014;10:2171–2192.
    • (2014) Autophagy , vol.10 , pp. 2171-2192
    • Poehler, A.M.1    Xiang, W.2    Spitzer, P.3
  • 69
    • 84879052241 scopus 로고    scopus 로고
    • Tubulin polymerization-promoting protein (TPPP/p25alpha) promotes unconventional secretion of alpha-synuclein through exophagy by impairing autophagosome-lysosome fusion
    • Ejlerskov P, Rasmussen I, Nielsen TT, et al. Tubulin polymerization-promoting protein (TPPP/p25alpha) promotes unconventional secretion of alpha-synuclein through exophagy by impairing autophagosome-lysosome fusion. J Biol Chem 2013;288:17313–17335.
    • (2013) J Biol Chem , vol.288 , pp. 17313-17335
    • Ejlerskov, P.1    Rasmussen, I.2    Nielsen, T.T.3
  • 70
    • 84899964982 scopus 로고    scopus 로고
    • Parkinson's disease-linked human PARK9/ATP13A2 maintains zinc homeostasis and promotes alpha-Synuclein externalization via exosomes
    • Kong SM, Chan BK, Park JS, et al. Parkinson's disease-linked human PARK9/ATP13A2 maintains zinc homeostasis and promotes alpha-Synuclein externalization via exosomes. Hum Mol Genet 2014;23:2816–2833.
    • (2014) Hum Mol Genet , vol.23 , pp. 2816-2833
    • Kong, S.M.1    Chan, B.K.2    Park, J.S.3
  • 71
    • 84909952796 scopus 로고    scopus 로고
    • ATP13A2/PARK9 regulates secretion of exosomes and alpha-synuclein
    • Tsunemi T, Hamada K, Krainc D. ATP13A2/PARK9 regulates secretion of exosomes and alpha-synuclein. J Neurosci 2014;34:15281–15287.
    • (2014) J Neurosci , vol.34 , pp. 15281-15287
    • Tsunemi, T.1    Hamada, K.2    Krainc, D.3
  • 72
    • 0031036896 scopus 로고    scopus 로고
    • Apoptosis and autophagy in nigral neurons of patients with Parkinson's disease
    • Anglade P, Vyas S, Javoy-Agid F, et al. Apoptosis and autophagy in nigral neurons of patients with Parkinson's disease. Histol Histopathol 1997;12:25–31.
    • (1997) Histol Histopathol , vol.12 , pp. 25-31
    • Anglade, P.1    Vyas, S.2    Javoy-Agid, F.3
  • 73
    • 0242499488 scopus 로고    scopus 로고
    • Localization of phosphorylated ERK/MAP kinases to mitochondria and autophagosomes in Lewy body diseases
    • Zhu JH, Guo F, Shelburne J, Watkins S, Chu CT. Localization of phosphorylated ERK/MAP kinases to mitochondria and autophagosomes in Lewy body diseases. Brain Pathol 2003;13:473–481.
    • (2003) Brain Pathol , vol.13 , pp. 473-481
    • Zhu, J.H.1    Guo, F.2    Shelburne, J.3    Watkins, S.4    Chu, C.T.5
  • 74
    • 68149123529 scopus 로고    scopus 로고
    • Alterations in lysosomal and proteasomal markers in Parkinson's disease: relationship to alpha-synuclein inclusions
    • Chu Y, Dodiya H, Aebischer P, Olanow CW, Kordower JH. Alterations in lysosomal and proteasomal markers in Parkinson's disease: relationship to alpha-synuclein inclusions. Neurobiol Dis 2009;35:385–398.
    • (2009) Neurobiol Dis , vol.35 , pp. 385-398
    • Chu, Y.1    Dodiya, H.2    Aebischer, P.3    Olanow, C.W.4    Kordower, J.H.5
  • 75
    • 77956855813 scopus 로고    scopus 로고
    • Pathogenic lysosomal depletion in Parkinson's disease
    • Dehay B, Bove J, Rodriguez-Muela N, et al. Pathogenic lysosomal depletion in Parkinson's disease. J Neurosci 2010;30:12535–12544.
    • (2010) J Neurosci , vol.30 , pp. 12535-12544
    • Dehay, B.1    Bove, J.2    Rodriguez-Muela, N.3
  • 76
    • 77949504405 scopus 로고    scopus 로고
    • Selective molecular alterations in the autophagy pathway in patients with Lewy body disease and in models of alpha-synucleinopathy
    • Crews L, Spencer B, Desplats P, et al. Selective molecular alterations in the autophagy pathway in patients with Lewy body disease and in models of alpha-synucleinopathy. PLoS One 2010;5:e9313.
    • (2010) PLoS One , vol.5
    • Crews, L.1    Spencer, B.2    Desplats, P.3
  • 77
    • 65849127844 scopus 로고    scopus 로고
    • Abberant alpha-synuclein confers toxicity to neurons in part through inhibition of chaperone-mediated autophagy
    • Xilouri M, Vogiatzi T, Vekrellis K, Park D, Stefanis L. Abberant alpha-synuclein confers toxicity to neurons in part through inhibition of chaperone-mediated autophagy. PLoS One 2009;4:e5515.
    • (2009) PLoS One , vol.4
    • Xilouri, M.1    Vogiatzi, T.2    Vekrellis, K.3    Park, D.4    Stefanis, L.5
  • 78
    • 79953202481 scopus 로고    scopus 로고
    • Mutant A53T alpha-synuclein induces neuronal death by increasing mitochondrial autophagy
    • Choubey V, Safiulina D, Vaarmann A, et al. Mutant A53T alpha-synuclein induces neuronal death by increasing mitochondrial autophagy. J Biol Chem 2011;286:10814–10824.
    • (2011) J Biol Chem , vol.286 , pp. 10814-10824
    • Choubey, V.1    Safiulina, D.2    Vaarmann, A.3
  • 79
    • 0035894855 scopus 로고    scopus 로고
    • Expression of A53T mutant but not wild-type alpha-synuclein in PC12 cells induces alterations of the ubiquitin-dependent degradation system, loss of dopamine release, and autophagic cell death
    • Stefanis L, Larsen KE, Rideout HJ, Sulzer D, Greene LA. Expression of A53T mutant but not wild-type alpha-synuclein in PC12 cells induces alterations of the ubiquitin-dependent degradation system, loss of dopamine release, and autophagic cell death. J Neurosci 2001;21:9549–9560.
    • (2001) J Neurosci , vol.21 , pp. 9549-9560
    • Stefanis, L.1    Larsen, K.E.2    Rideout, H.J.3    Sulzer, D.4    Greene, L.A.5
  • 80
    • 70350550208 scopus 로고    scopus 로고
    • Beclin 1 gene transfer activates autophagy and ameliorates the neurodegenerative pathology in alpha-synuclein models of Parkinson's and Lewy body diseases
    • Spencer B, Potkar R, Trejo M, et al. Beclin 1 gene transfer activates autophagy and ameliorates the neurodegenerative pathology in alpha-synuclein models of Parkinson's and Lewy body diseases. J Neurosci 2009;29:13578–13588.
    • (2009) J Neurosci , vol.29 , pp. 13578-13588
    • Spencer, B.1    Potkar, R.2    Trejo, M.3
  • 81
    • 77957189194 scopus 로고    scopus 로고
    • alpha-Synuclein impairs macroautophagy: implications for Parkinson's disease
    • Winslow AR, Chen CW, Corrochano S, et al. alpha-Synuclein impairs macroautophagy: implications for Parkinson's disease. J Cell Biol 2010;190:1023–1037.
    • (2010) J Cell Biol , vol.190 , pp. 1023-1037
    • Winslow, A.R.1    Chen, C.W.2    Corrochano, S.3
  • 82
    • 84894350781 scopus 로고    scopus 로고
    • HMGB1 is involved in autophagy inhibition caused by SNCA/alpha-synuclein overexpression: a process modulated by the natural autophagy inducer corynoxine B
    • Song JX, Lu JH, Liu LF, et al. HMGB1 is involved in autophagy inhibition caused by SNCA/alpha-synuclein overexpression: a process modulated by the natural autophagy inducer corynoxine B. Autophagy 2014;10:144–154.
    • (2014) Autophagy , vol.10 , pp. 144-154
    • Song, J.X.1    Lu, J.H.2    Liu, L.F.3
  • 83
    • 84911001724 scopus 로고    scopus 로고
    • Overexpression of human E46K mutant alpha-synuclein impairs macroautophagy via inactivation of JNK1-Bcl-2 pathway
    • Yan JQ, Yuan YH, Gao YN, et al. Overexpression of human E46K mutant alpha-synuclein impairs macroautophagy via inactivation of JNK1-Bcl-2 pathway. Mol Neurobiol 2014;50:685–701.
    • (2014) Mol Neurobiol , vol.50 , pp. 685-701
    • Yan, J.Q.1    Yuan, Y.H.2    Gao, Y.N.3
  • 84
    • 84921456454 scopus 로고    scopus 로고
    • A53T human alpha-synuclein overexpression in transgenic mice induces pervasive mitochondria macroautophagy defects preceding dopamine neuron degeneration
    • Chen L, Xie Z, Turkson S, Zhuang X. A53T human alpha-synuclein overexpression in transgenic mice induces pervasive mitochondria macroautophagy defects preceding dopamine neuron degeneration. J Neurosci 2015;35:890–905.
    • (2015) J Neurosci , vol.35 , pp. 890-905
    • Chen, L.1    Xie, Z.2    Turkson, S.3    Zhuang, X.4
  • 85
    • 84989360055 scopus 로고    scopus 로고
    • Alpha-Synuclein affects neurite morphology, autophagy, vesicle transport and axonal degeneration in CNS neurons
    • Koch JC, Bitow F, Haack J, et al. Alpha-Synuclein affects neurite morphology, autophagy, vesicle transport and axonal degeneration in CNS neurons. Cell Death Dis 2015;6:e1811.
    • (2015) Cell Death Dis , vol.6
    • Koch, J.C.1    Bitow, F.2    Haack, J.3
  • 86
    • 84919468220 scopus 로고    scopus 로고
    • Formation of alpha-synuclein Lewy neurite-like aggregates in axons impedes the transport of distinct endosomes
    • Volpicelli-Daley LA, Gamble KL, Schultheiss CE, Riddle DM, West AB, Lee VM. Formation of alpha-synuclein Lewy neurite-like aggregates in axons impedes the transport of distinct endosomes. Mol Biol Cell 2014;25:4010–4023.
    • (2014) Mol Biol Cell , vol.25 , pp. 4010-4023
    • Volpicelli-Daley, L.A.1    Gamble, K.L.2    Schultheiss, C.E.3    Riddle, D.M.4    West, A.B.5    Lee, V.M.6
  • 87
    • 85012106645 scopus 로고    scopus 로고
    • Role of alpha- and beta-synucleins in the axonal pathology of Parkinson's disease and related synucleinopathies
    • Sekigawa A, Takamatsu Y, Sekiyama K, Hashimoto M. Role of alpha- and beta-synucleins in the axonal pathology of Parkinson's disease and related synucleinopathies. Biomolecules 2015;5:1000–1011.
    • (2015) Biomolecules , vol.5 , pp. 1000-1011
    • Sekigawa, A.1    Takamatsu, Y.2    Sekiyama, K.3    Hashimoto, M.4
  • 88
    • 84863877366 scopus 로고    scopus 로고
    • Involvement of macroautophagy in multiple system atrophy and protein aggregate formation in oligodendrocytes
    • Schwarz L, Goldbaum O, Bergmann M, Probst-Cousin S, Richter-Landsberg C. Involvement of macroautophagy in multiple system atrophy and protein aggregate formation in oligodendrocytes. J Mol Neurosci 2012;47:256–266.
    • (2012) J Mol Neurosci , vol.47 , pp. 256-266
    • Schwarz, L.1    Goldbaum, O.2    Bergmann, M.3    Probst-Cousin, S.4    Richter-Landsberg, C.5
  • 89
    • 84866533589 scopus 로고    scopus 로고
    • Alteration of autophagosomal proteins in the brain of multiple system atrophy
    • Tanji K, Odagiri S, Maruyama A, et al. Alteration of autophagosomal proteins in the brain of multiple system atrophy. Neurobiol Dis 2013;49:190–198.
    • (2013) Neurobiol Dis , vol.49 , pp. 190-198
    • Tanji, K.1    Odagiri, S.2    Maruyama, A.3
  • 90
    • 84866444893 scopus 로고    scopus 로고
    • Immunohistochemical localization of aggresomal proteins in glial cytoplasmic inclusions in multiple system atrophy
    • Chiba Y, Takei S, Kawamura N, et al. Immunohistochemical localization of aggresomal proteins in glial cytoplasmic inclusions in multiple system atrophy. Neuropathol Appl Neurobiol 2012;38:559–571.
    • (2012) Neuropathol Appl Neurobiol , vol.38 , pp. 559-571
    • Chiba, Y.1    Takei, S.2    Kawamura, N.3
  • 91
    • 78149469728 scopus 로고    scopus 로고
    • Chaperone-mediated autophagy markers in Parkinson disease brains
    • Alvarez-Erviti L, Rodriguez-Oroz MC, Cooper JM, et al. Chaperone-mediated autophagy markers in Parkinson disease brains. Arch Neurol 2010;67:1464–1472.
    • (2010) Arch Neurol , vol.67 , pp. 1464-1472
    • Alvarez-Erviti, L.1    Rodriguez-Oroz, M.C.2    Cooper, J.M.3
  • 93
    • 84937677490 scopus 로고    scopus 로고
    • VPS35 in dopamine neurons is required for endosome-to-Golgi retrieval of Lamp2a, a receptor of chaperone-mediated autophagy that is critical for alpha-synuclein degradation and prevention of pathogenesis of Parkinson's disease
    • Tang FL, Erion JR, Tian Y, et al. VPS35 in dopamine neurons is required for endosome-to-Golgi retrieval of Lamp2a, a receptor of chaperone-mediated autophagy that is critical for alpha-synuclein degradation and prevention of pathogenesis of Parkinson's disease. J Neurosci 2015;35:10613–10628.
    • (2015) J Neurosci , vol.35 , pp. 10613-10628
    • Tang, F.L.1    Erion, J.R.2    Tian, Y.3
  • 94
    • 58149215720 scopus 로고    scopus 로고
    • Regulation of neuronal survival factor MEF2D by chaperone-mediated autophagy
    • Yang Q, She H, Gearing M, et al. Regulation of neuronal survival factor MEF2D by chaperone-mediated autophagy. Science 2009;323:124–127.
    • (2009) Science , vol.323 , pp. 124-127
    • Yang, Q.1    She, H.2    Gearing, M.3
  • 95
    • 84929705440 scopus 로고    scopus 로고
    • Lysosomal-associated membrane protein 2 isoforms are differentially affected in early Parkinson's disease
    • Murphy KE, Gysbers AM, Abbott SK, et al. Lysosomal-associated membrane protein 2 isoforms are differentially affected in early Parkinson's disease. Mov Disord 2015;30:1639–1647.
    • (2015) Mov Disord , vol.30 , pp. 1639-1647
    • Murphy, K.E.1    Gysbers, A.M.2    Abbott, S.K.3
  • 96
    • 84894528843 scopus 로고    scopus 로고
    • Reduced glucocerebrosidase is associated with increased alpha-synuclein in sporadic Parkinson's disease
    • Murphy KE, Gysbers AM, Abbott SK, et al. Reduced glucocerebrosidase is associated with increased alpha-synuclein in sporadic Parkinson's disease. Brain 2014;137(Pt 3):834–848.
    • (2014) Brain , vol.137 , pp. 834-848
    • Murphy, K.E.1    Gysbers, A.M.2    Abbott, S.K.3
  • 98
    • 84908352032 scopus 로고    scopus 로고
    • Targeted suppression of chaperone-mediated autophagy by miR-320a promotes alpha-synuclein aggregation
    • Li G, Yang H, Zhu D, Huang H, Liu G, Lun P. Targeted suppression of chaperone-mediated autophagy by miR-320a promotes alpha-synuclein aggregation. Int J Mol Sci 2014;15:15845–15857.
    • (2014) Int J Mol Sci , vol.15 , pp. 15845-15857
    • Li, G.1    Yang, H.2    Zhu, D.3    Huang, H.4    Liu, G.5    Lun, P.6
  • 99
    • 85017330629 scopus 로고    scopus 로고
    • LAMP-2 deficiency leads to hippocampal dysfunction but normal clearance of neuronal substrates of chaperone-mediated autophagy in a mouse model for Danon disease
    • Rothaug M, Stroobants S, Schweizer M, et al. LAMP-2 deficiency leads to hippocampal dysfunction but normal clearance of neuronal substrates of chaperone-mediated autophagy in a mouse model for Danon disease. Acta Neuropathol Commun 2015;3:6.
    • (2015) Acta Neuropathol Commun , vol.3 , pp. 6
    • Rothaug, M.1    Stroobants, S.2    Schweizer, M.3
  • 100
    • 3042760943 scopus 로고    scopus 로고
    • Disturbed cholesterol traffic but normal proteolytic function in LAMP-1/LAMP-2 double-deficient fibroblasts
    • Eskelinen EL, Schmidt CK, Neu S, et al. Disturbed cholesterol traffic but normal proteolytic function in LAMP-1/LAMP-2 double-deficient fibroblasts. Mol Biol Cell 2004;15:3132–3145.
    • (2004) Mol Biol Cell , vol.15 , pp. 3132-3145
    • Eskelinen, E.L.1    Schmidt, C.K.2    Neu, S.3
  • 101
    • 67650087652 scopus 로고    scopus 로고
    • Glucocerebrosidase mutations in clinical and pathologically proven Parkinson's disease
    • Neumann J, Bras J, Deas E, et al. Glucocerebrosidase mutations in clinical and pathologically proven Parkinson's disease. Brain 2009;132(Pt 7):1783–1794.
    • (2009) Brain , vol.132 , pp. 1783-1794
    • Neumann, J.1    Bras, J.2    Deas, E.3
  • 102
    • 79956199921 scopus 로고    scopus 로고
    • Acid beta-glucosidase mutants linked to gaucher disease, parkinson disease, and lewy body dementia alter alpha-synuclein processing
    • Cullen V, Sardi SP, Ng J, et al. Acid beta-glucosidase mutants linked to gaucher disease, parkinson disease, and lewy body dementia alter alpha-synuclein processing. Ann Neurol 2011;69:940–953.
    • (2011) Ann Neurol , vol.69 , pp. 940-953
    • Cullen, V.1    Sardi, S.P.2    Ng, J.3
  • 103
    • 71049138581 scopus 로고    scopus 로고
    • Alpha-synuclein-glucocerebrosidase interactions in pharmacological Gaucher models: a biological link between Gaucher disease and parkinsonism
    • Manning-Bog AB, Schule B, Langston JW. Alpha-synuclein-glucocerebrosidase interactions in pharmacological Gaucher models: a biological link between Gaucher disease and parkinsonism. Neurotoxicology 2009;30:1127–1132.
    • (2009) Neurotoxicology , vol.30 , pp. 1127-1132
    • Manning-Bog, A.B.1    Schule, B.2    Langston, J.W.3
  • 104
    • 84875967929 scopus 로고    scopus 로고
    • Loss of beta-glucocerebrosidase activity does not affect alpha-synuclein levels or lysosomal function in neuronal cells
    • Dermentzaki G, Dimitriou E, Xilouri M, Michelakakis H, Stefanis L. Loss of beta-glucocerebrosidase activity does not affect alpha-synuclein levels or lysosomal function in neuronal cells. PLoS One 2013;8:e60674.
    • (2013) PLoS One , vol.8
    • Dermentzaki, G.1    Dimitriou, E.2    Xilouri, M.3    Michelakakis, H.4    Stefanis, L.5
  • 105
    • 84870671394 scopus 로고    scopus 로고
    • Glucocerebrosidase inhibition causes mitochondrial dysfunction and free radical damage
    • Cleeter MW, Chau KY, Gluck C, et al. Glucocerebrosidase inhibition causes mitochondrial dysfunction and free radical damage. Neurochem Int 2013;62:1–7.
    • (2013) Neurochem Int , vol.62 , pp. 1-7
    • Cleeter, M.W.1    Chau, K.Y.2    Gluck, C.3
  • 106
    • 79952619654 scopus 로고    scopus 로고
    • Accumulation and distribution of alpha-synuclein and ubiquitin in the CNS of Gaucher disease mouse models
    • Xu YH, Sun Y, Ran H, Quinn B, Witte D, Grabowski GA. Accumulation and distribution of alpha-synuclein and ubiquitin in the CNS of Gaucher disease mouse models. Mol Genet Metab 2011;102:436–447.
    • (2011) Mol Genet Metab , vol.102 , pp. 436-447
    • Xu, Y.H.1    Sun, Y.2    Ran, H.3    Quinn, B.4    Witte, D.5    Grabowski, G.A.6
  • 107
    • 84922266926 scopus 로고    scopus 로고
    • Augmentation of phenotype in a transgenic Parkinson mouse heterozygous for a Gaucher mutation
    • Fishbein I, Kuo YM, Giasson BI, Nussbaum RL. Augmentation of phenotype in a transgenic Parkinson mouse heterozygous for a Gaucher mutation. Brain 2014;137(Pt 12):3235–3247.
    • (2014) Brain , vol.137 , pp. 3235-3247
    • Fishbein, I.1    Kuo, Y.M.2    Giasson, B.I.3    Nussbaum, R.L.4
  • 108
    • 84912058317 scopus 로고    scopus 로고
    • iPSC-derived dopamine neurons reveal differences between monozygotic twins discordant for Parkinson's disease
    • Woodard CM, Campos BA, Kuo SH, et al. iPSC-derived dopamine neurons reveal differences between monozygotic twins discordant for Parkinson's disease. Cell Rep 2014;9:1173–1182.
    • (2014) Cell Rep , vol.9 , pp. 1173-1182
    • Woodard, C.M.1    Campos, B.A.2    Kuo, S.H.3
  • 109
    • 84902201548 scopus 로고    scopus 로고
    • iPSC-derived neurons from GBA1-associated Parkinson's disease patients show autophagic defects and impaired calcium homeostasis
    • Schondorf DC, Aureli M, McAllister FE, et al. iPSC-derived neurons from GBA1-associated Parkinson's disease patients show autophagic defects and impaired calcium homeostasis. Nat Commun 2014;5:4028.
    • (2014) Nat Commun , vol.5 , pp. 4028
    • Schondorf, D.C.1    Aureli, M.2    McAllister, F.E.3
  • 110
    • 84907360500 scopus 로고    scopus 로고
    • Glucocerebrosidase depletion enhances cell-to-cell transmission of alpha-synuclein
    • Bae EJ, Yang NY, Song M, et al. Glucocerebrosidase depletion enhances cell-to-cell transmission of alpha-synuclein. Nat Commun 2014;5:4755.
    • (2014) Nat Commun , vol.5 , pp. 4755
    • Bae, E.J.1    Yang, N.Y.2    Song, M.3
  • 111
    • 84965185844 scopus 로고    scopus 로고
    • Loss of glucocerebrosidase 1 activity causes lysosomal dysfunction and alpha-synuclein aggregation
    • Bae EJ, Yang NY, Lee C, et al. Loss of glucocerebrosidase 1 activity causes lysosomal dysfunction and alpha-synuclein aggregation. Exp Mol Med 2015;47:e153.
    • (2015) Exp Mol Med , vol.47
    • Bae, E.J.1    Yang, N.Y.2    Lee, C.3
  • 112
    • 79959925894 scopus 로고    scopus 로고
    • {alpha}-Synuclein interacts with glucocerebrosidase providing a molecular link between Parkinson and Gaucher diseases
    • Yap TL, Gruschus JM, Velayati A, et al. {alpha}-Synuclein interacts with glucocerebrosidase providing a molecular link between Parkinson and Gaucher diseases. J Biol Chem 2011;286:28080–28088.
    • (2011) J Biol Chem , vol.286 , pp. 28080-28088
    • Yap, T.L.1    Gruschus, J.M.2    Velayati, A.3
  • 113
    • 79960009804 scopus 로고    scopus 로고
    • Gaucher disease glucocerebrosidase and alpha-synuclein form a bidirectional pathogenic loop in synucleinopathies
    • Mazzulli JR, Xu YH, Sun Y, et al. Gaucher disease glucocerebrosidase and alpha-synuclein form a bidirectional pathogenic loop in synucleinopathies. Cell 2011;146:37–52.
    • (2011) Cell , vol.146 , pp. 37-52
    • Mazzulli, J.R.1    Xu, Y.H.2    Sun, Y.3
  • 114
    • 84867036900 scopus 로고    scopus 로고
    • Glucocerebrosidase deficiency in substantia nigra of Parkinson disease brains
    • Gegg ME, Burke D, Heales SJ, et al. Glucocerebrosidase deficiency in substantia nigra of Parkinson disease brains. Ann Neurol 2012;72:455–463.
    • (2012) Ann Neurol , vol.72 , pp. 455-463
    • Gegg, M.E.1    Burke, D.2    Heales, S.J.3
  • 115
    • 84874487118 scopus 로고    scopus 로고
    • Augmenting CNS glucocerebrosidase activity as a therapeutic strategy for parkinsonism and other Gaucher-related synucleinopathies
    • Sardi SP, Clarke J, Viel C, et al. Augmenting CNS glucocerebrosidase activity as a therapeutic strategy for parkinsonism and other Gaucher-related synucleinopathies. Proc Natl Acad Sci U S A 2013;110:3537–3542.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 3537-3542
    • Sardi, S.P.1    Clarke, J.2    Viel, C.3
  • 116
    • 84908282747 scopus 로고    scopus 로고
    • LIMP-2 expression is critical for beta-glucocerebrosidase activity and alpha-synuclein clearance
    • Rothaug M, Zunke F, Mazzulli JR, et al. LIMP-2 expression is critical for beta-glucocerebrosidase activity and alpha-synuclein clearance. Proc Natl Acad Sci U S A 2014;111:15573–15578.
    • (2014) Proc Natl Acad Sci U S A , vol.111 , pp. 15573-15578
    • Rothaug, M.1    Zunke, F.2    Mazzulli, J.R.3
  • 117
    • 84858276817 scopus 로고    scopus 로고
    • Evidence of an association between the scavenger receptor class B member 2 gene and Parkinson's disease
    • Michelakakis H, Xiromerisiou G, Dardiotis E, et al. Evidence of an association between the scavenger receptor class B member 2 gene and Parkinson's disease. Mov Disord 2012;27:400–405.
    • (2012) Mov Disord , vol.27 , pp. 400-405
    • Michelakakis, H.1    Xiromerisiou, G.2    Dardiotis, E.3
  • 118
    • 79959841853 scopus 로고    scopus 로고
    • Web-based genome-wide association study identifies two novel loci and a substantial genetic component for Parkinson's disease
    • Do CB, Tung JY, Dorfman E, et al. Web-based genome-wide association study identifies two novel loci and a substantial genetic component for Parkinson's disease. PLoS Genet 2011;7:e1002141.
    • (2011) PLoS Genet , vol.7
    • Do, C.B.1    Tung, J.Y.2    Dorfman, E.3
  • 119
    • 84876104005 scopus 로고    scopus 로고
    • The role of SCARB2 as susceptibility factor in Parkinson's disease
    • Hopfner F, Schulte EC, Mollenhauer B, et al. The role of SCARB2 as susceptibility factor in Parkinson's disease. Mov Disord 2013;28:538–540.
    • (2013) Mov Disord , vol.28 , pp. 538-540
    • Hopfner, F.1    Schulte, E.C.2    Mollenhauer, B.3
  • 120
    • 84860233638 scopus 로고    scopus 로고
    • Association study of SCARB2 rs6812193 polymorphism with Parkinson's disease in Han Chinese
    • Chen S, Zhang Y, Chen W, et al. Association study of SCARB2 rs6812193 polymorphism with Parkinson's disease in Han Chinese. Neurosci Lett 2012;516:21–23.
    • (2012) Neurosci Lett , vol.516 , pp. 21-23
    • Chen, S.1    Zhang, Y.2    Chen, W.3
  • 121
    • 84875245748 scopus 로고    scopus 로고
    • Is Parkinson disease associated with lysosomal integral membrane protein type-2?: challenges in interpreting association data
    • Maniwang E, Tayebi N, Sidransky E. Is Parkinson disease associated with lysosomal integral membrane protein type-2?: challenges in interpreting association data. Mol Genet Metab 2013;108:269–271.
    • (2013) Mol Genet Metab , vol.108 , pp. 269-271
    • Maniwang, E.1    Tayebi, N.2    Sidransky, E.3
  • 123
    • 84925597891 scopus 로고    scopus 로고
    • Genetic and chemical activation of TFEB mediates clearance of aggregated alpha-synuclein
    • Kilpatrick K, Zeng Y, Hancock T, Segatori L. Genetic and chemical activation of TFEB mediates clearance of aggregated alpha-synuclein. PLoS One 2015;10:e0120819.
    • (2015) PLoS One , vol.10
    • Kilpatrick, K.1    Zeng, Y.2    Hancock, T.3    Segatori, L.4
  • 124
    • 34247161367 scopus 로고    scopus 로고
    • Trehalose, a novel mTOR-independent autophagy enhancer, accelerates the clearance of mutant huntingtin and alpha-synuclein
    • Sarkar S, Davies JE, Huang Z, Tunnacliffe A, Rubinsztein DC. Trehalose, a novel mTOR-independent autophagy enhancer, accelerates the clearance of mutant huntingtin and alpha-synuclein. J Biol Chem 2007;282:5641–5652.
    • (2007) J Biol Chem , vol.282 , pp. 5641-5652
    • Sarkar, S.1    Davies, J.E.2    Huang, Z.3    Tunnacliffe, A.4    Rubinsztein, D.C.5
  • 125
    • 84925485842 scopus 로고    scopus 로고
    • 3-anhydro-6-hydroxy-ophiobolin A, a fungal sesterterpene from Bipolaris oryzae induced autophagy and promoted the degradation of alpha-synuclein in PC12 cells
    • Xue D, Wang Q, Chen Z, et al. 3-anhydro-6-hydroxy-ophiobolin A, a fungal sesterterpene from Bipolaris oryzae induced autophagy and promoted the degradation of alpha-synuclein in PC12 cells. Bioorg Med Chem Lett 2015;25:1464–1470.
    • (2015) Bioorg Med Chem Lett , vol.25 , pp. 1464-1470
    • Xue, D.1    Wang, Q.2    Chen, Z.3
  • 126
    • 84929448327 scopus 로고    scopus 로고
    • Treatment with trehalose prevents behavioral and neurochemical deficits produced in an AAV alpha-synuclein rat model of Parkinson's disease
    • May 14., [Epub ahead of print]
    • He Q, Koprich JB, Wang Y, et al. Treatment with trehalose prevents behavioral and neurochemical deficits produced in an AAV alpha-synuclein rat model of Parkinson's disease. Mol Neurobiol 2015 May 14. doi: 10.1007/s12035-015-9173-7. [Epub ahead of print]
    • (2015) Mol Neurobiol
    • He, Q.1    Koprich, J.B.2    Wang, Y.3
  • 127
    • 84881250979 scopus 로고    scopus 로고
    • Nilotinib reverses loss of dopamine neurons and improves motor behavior via autophagic degradation of alpha-synuclein in Parkinson's disease models
    • Hebron ML, Lonskaya I, Moussa CE. Nilotinib reverses loss of dopamine neurons and improves motor behavior via autophagic degradation of alpha-synuclein in Parkinson's disease models. Hum Mol Genet 2013;22:3315–3328.
    • (2013) Hum Mol Genet , vol.22 , pp. 3315-3328
    • Hebron, M.L.1    Lonskaya, I.2    Moussa, C.E.3
  • 128
    • 84899894003 scopus 로고    scopus 로고
    • c-Abl phosphorylates alpha-synuclein and regulates its degradation: implication for alpha-synuclein clearance and contribution to the pathogenesis of Parkinson's disease
    • Mahul-Mellier AL, Fauvet B, Gysbers A, et al. c-Abl phosphorylates alpha-synuclein and regulates its degradation: implication for alpha-synuclein clearance and contribution to the pathogenesis of Parkinson's disease. Hum Mol Genet 2014;23:2858–2879.
    • (2014) Hum Mol Genet , vol.23 , pp. 2858-2879
    • Mahul-Mellier, A.L.1    Fauvet, B.2    Gysbers, A.3
  • 129
    • 34250183177 scopus 로고    scopus 로고
    • HDAC6 rescues neurodegeneration and provides an essential link between autophagy and the UPS
    • Pandey UB, Nie Z, Batlevi Y, et al. HDAC6 rescues neurodegeneration and provides an essential link between autophagy and the UPS. Nature 2007;447:859–863.
    • (2007) Nature , vol.447 , pp. 859-863
    • Pandey, U.B.1    Nie, Z.2    Batlevi, Y.3
  • 130
    • 65249125897 scopus 로고    scopus 로고
    • p53 mediates mitochondria dysfunction-triggered autophagy activation and cell death in rat striatum
    • Zhang XD, Wang Y, Wang Y, et al. p53 mediates mitochondria dysfunction-triggered autophagy activation and cell death in rat striatum. Autophagy 2009;5:339–350.
    • (2009) Autophagy , vol.5 , pp. 339-350
    • Zhang, X.D.1    Wang, Y.2    Wang, Y.3
  • 131
    • 84859702745 scopus 로고    scopus 로고
    • Differential effects of UCHL1 modulation on alpha-synuclein in PD-like models of alpha-synucleinopathy
    • Cartier AE, Ubhi K, Spencer B, et al. Differential effects of UCHL1 modulation on alpha-synuclein in PD-like models of alpha-synucleinopathy. PLoS One 2012;7:e34713.
    • (2012) PLoS One , vol.7
    • Cartier, A.E.1    Ubhi, K.2    Spencer, B.3
  • 132
    • 77955023765 scopus 로고    scopus 로고
    • Ubiquilin functions in autophagy and is degraded by chaperone-mediated autophagy
    • Rothenberg C, Srinivasan D, Mah L, et al. Ubiquilin functions in autophagy and is degraded by chaperone-mediated autophagy. Hum Mol Genet 2010;19:3219–3232.
    • (2010) Hum Mol Genet , vol.19 , pp. 3219-3232
    • Rothenberg, C.1    Srinivasan, D.2    Mah, L.3
  • 133
    • 77957674939 scopus 로고    scopus 로고
    • Ubiquilin at a crossroads in protein degradation pathways
    • Rothenberg C, Monteiro MJ. Ubiquilin at a crossroads in protein degradation pathways. Autophagy 2010;6:979–980.
    • (2010) Autophagy , vol.6 , pp. 979-980
    • Rothenberg, C.1    Monteiro, M.J.2
  • 135
    • 48249091611 scopus 로고    scopus 로고
    • Constitutive activation of chaperone-mediated autophagy in cells with impaired macroautophagy
    • Kaushik S, Massey AC, Mizushima N, Cuervo AM. Constitutive activation of chaperone-mediated autophagy in cells with impaired macroautophagy. Mol Biol Cell 2008;19:2179–2192.
    • (2008) Mol Biol Cell , vol.19 , pp. 2179-2192
    • Kaushik, S.1    Massey, A.C.2    Mizushima, N.3    Cuervo, A.M.4
  • 136
    • 41949125675 scopus 로고    scopus 로고
    • Loss of macroautophagy promotes or prevents fibroblast apoptosis depending on the death stimulus
    • Wang Y, Singh R, Massey AC, et al. Loss of macroautophagy promotes or prevents fibroblast apoptosis depending on the death stimulus. J Biol Chem 2008;283:4766–4777.
    • (2008) J Biol Chem , vol.283 , pp. 4766-4777
    • Wang, Y.1    Singh, R.2    Massey, A.C.3
  • 138
    • 51349095898 scopus 로고    scopus 로고
    • Restoration of chaperone-mediated autophagy in aging liver improves cellular maintenance and hepatic function
    • Zhang C, Cuervo AM. Restoration of chaperone-mediated autophagy in aging liver improves cellular maintenance and hepatic function. Nat Med 2008;14:959–965.
    • (2008) Nat Med , vol.14 , pp. 959-965
    • Zhang, C.1    Cuervo, A.M.2
  • 139
    • 84879962810 scopus 로고    scopus 로고
    • Boosting chaperone-mediated autophagy in vivo mitigates alpha-synuclein-induced neurodegeneration
    • Xilouri M, Brekk OR, Landeck N, et al. Boosting chaperone-mediated autophagy in vivo mitigates alpha-synuclein-induced neurodegeneration. Brain 2013;136(Pt 7):2130–2146.
    • (2013) Brain , vol.136 , pp. 2130-2146
    • Xilouri, M.1    Brekk, O.R.2    Landeck, N.3
  • 140
    • 84902546681 scopus 로고    scopus 로고
    • In silico modeling of the effects of alpha-synuclein oligomerization on dopaminergic neuronal homeostasis
    • Ouzounoglou E, Kalamatianos D, Emmanouilidou E, et al. In silico modeling of the effects of alpha-synuclein oligomerization on dopaminergic neuronal homeostasis. BMC Syst Biol 2014;8:54.
    • (2014) BMC Syst Biol , vol.8 , pp. 54
    • Ouzounoglou, E.1    Kalamatianos, D.2    Emmanouilidou, E.3
  • 142
    • 79961083395 scopus 로고    scopus 로고
    • CNS expression of glucocerebrosidase corrects {alpha}-synuclein pathology and memory in a mouse model of Gaucher-related synucleinopathy
    • Sardi SP, Clarke J, Kinnecom C, et al. CNS expression of glucocerebrosidase corrects {alpha}-synuclein pathology and memory in a mouse model of Gaucher-related synucleinopathy. Proc Natl Acad Sci U S A 2011;108:12101–12106.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 12101-12106
    • Sardi, S.P.1    Clarke, J.2    Kinnecom, C.3
  • 143
    • 84907486116 scopus 로고    scopus 로고
    • Development of targeted therapies for Parkinson's disease and related synucleinopathies
    • Sybertz E, Krainc D. Development of targeted therapies for Parkinson's disease and related synucleinopathies. J Lipid Res 2014;55:1996–2003.
    • (2014) J Lipid Res , vol.55 , pp. 1996-2003
    • Sybertz, E.1    Krainc, D.2
  • 144
    • 33947376087 scopus 로고    scopus 로고
    • Selective action of the iminosugar isofagomine, a pharmacological chaperone for mutant forms of acid-beta-glucosidase
    • Steet R, Chung S, Lee WS, Pine CW, Do H, Kornfeld S. Selective action of the iminosugar isofagomine, a pharmacological chaperone for mutant forms of acid-beta-glucosidase. Biochem Pharmacol 2007;73:1376–1383.
    • (2007) Biochem Pharmacol , vol.73 , pp. 1376-1383
    • Steet, R.1    Chung, S.2    Lee, W.S.3    Pine, C.W.4    Do, H.5    Kornfeld, S.6
  • 145
    • 33748801230 scopus 로고    scopus 로고
    • The iminosugar isofagomine increases the activity of N370S mutant acid beta-glucosidase in Gaucher fibroblasts by several mechanisms
    • Steet RA, Chung S, Wustman B, Powe A, Do H, Kornfeld SA. The iminosugar isofagomine increases the activity of N370S mutant acid beta-glucosidase in Gaucher fibroblasts by several mechanisms. Proc Natl Acad Sci U S A 2006;103:13813–13818.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 13813-13818
    • Steet, R.A.1    Chung, S.2    Wustman, B.3    Powe, A.4    Do, H.5    Kornfeld, S.A.6
  • 146
    • 84919876441 scopus 로고    scopus 로고
    • A GCase chaperone improves motor function in a mouse model of synucleinopathy
    • Richter F, Fleming SM, Watson M, et al. A GCase chaperone improves motor function in a mouse model of synucleinopathy. Neurotherapeutics 2014;11:840–856.
    • (2014) Neurotherapeutics , vol.11 , pp. 840-856
    • Richter, F.1    Fleming, S.M.2    Watson, M.3
  • 147
    • 84899819100 scopus 로고    scopus 로고
    • Ambroxol improves lysosomal biochemistry in glucocerebrosidase mutation-linked Parkinson disease cells
    • McNeill A, Magalhaes J, Shen C, et al. Ambroxol improves lysosomal biochemistry in glucocerebrosidase mutation-linked Parkinson disease cells. Brain 2014;137(Pt 5):1481–1495.
    • (2014) Brain , vol.137 , pp. 1481-1495
    • McNeill, A.1    Magalhaes, J.2    Shen, C.3


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