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Volumn 30, Issue 8, 2015, Pages 1026-1033

A new role for α-synuclein in Parkinson's disease: Alteration of ER–mitochondrial communication

Author keywords

MAM; Parkinson's Disease; synuclein

Indexed keywords

ALPHA SYNUCLEIN;

EID: 84929783342     PISSN: 08853185     EISSN: 15318257     Source Type: Journal    
DOI: 10.1002/mds.26239     Document Type: Article
Times cited : (62)

References (130)
  • 1
    • 10544234193 scopus 로고    scopus 로고
    • Mapping of a gene for Parkinson's disease to chromosome 4q21-q23
    • Polymeropoulos MH, Higgins JJ, Golbe LI, et al. Mapping of a gene for Parkinson's disease to chromosome 4q21-q23. Science 1996;274:1197-1199.
    • (1996) Science , vol.274 , pp. 1197-1199
    • Polymeropoulos, M.H.1    Higgins, J.J.2    Golbe, L.I.3
  • 2
    • 0030744876 scopus 로고    scopus 로고
    • Mutation in the α-synuclein gene identified in families with Parkinson's disease
    • Polymeropoulos MH, Lavedan C, Leroy E, et al. Mutation in the α-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
  • 3
    • 0033365388 scopus 로고    scopus 로고
    • Genetic analysis of families with Parkinson disease that carry the Ala53Thr mutation in the gene encoding α-synuclein
    • Athanassiadou A, Voutsinas G, Psiouri L, et al. Genetic analysis of families with Parkinson disease that carry the Ala53Thr mutation in the gene encoding α-synuclein. Am J Hum Genet 1999;65:555-558.
    • (1999) Am J Hum Genet , vol.65 , pp. 555-558
    • Athanassiadou, A.1    Voutsinas, G.2    Psiouri, L.3
  • 4
    • 0035097503 scopus 로고    scopus 로고
    • Clinical and pathological features of a Parkinsonian syndrome in a family with an Ala53Thr α-synuclein mutation
    • Spira PJ, Sharpe DM, Halliday G, et al. Clinical and pathological features of a Parkinsonian syndrome in a family with an Ala53Thr α-synuclein mutation. Ann Neurol 2001;49:313-319.
    • (2001) Ann Neurol , vol.49 , pp. 313-319
    • Spira, P.J.1    Sharpe, D.M.2    Halliday, G.3
  • 5
    • 34248351183 scopus 로고    scopus 로고
    • The Ala53Thr mutation in the α-synuclein gene in a Korean family with Parkinson disease
    • Ki C-S, Stavrou EF, Davanos N, et al. The Ala53Thr mutation in the α-synuclein gene in a Korean family with Parkinson disease. Clin Genet 2007;71:471-473.
    • (2007) Clin Genet , vol.71 , pp. 471-473
    • Ki, C.-S.1    Stavrou, E.F.2    Davanos, N.3
  • 6
    • 52649172690 scopus 로고    scopus 로고
    • Analysis of PARK genes in a Korean cohort of early-onset Parkinson disease
    • Choi JM, Woo MS, Ma H-I, et al. Analysis of PARK genes in a Korean cohort of early-onset Parkinson disease. Neurogenetics 2008;9:263-269.
    • (2008) Neurogenetics , vol.9 , pp. 263-269
    • Choi, J.M.1    Woo, M.S.2    Ma, H.-I.3
  • 7
    • 70350149351 scopus 로고    scopus 로고
    • A Swedish family with de novo α-synuclein A53T mutation: evidence for early cortical dysfunction
    • Puschmann A, Ross OA, Vilariño-Güell C, et al. A Swedish family with de novo α-synuclein A53T mutation: evidence for early cortical dysfunction. Parkinsonism Relat Disord 2009;15:627-632.
    • (2009) Parkinsonism Relat Disord , vol.15 , pp. 627-632
    • Puschmann, A.1    Ross, O.A.2    Vilariño-Güell, C.3
  • 8
    • 0031990490 scopus 로고    scopus 로고
    • Ala30Pro mutation in the gene encoding α-synuclein in Parkinson's disease
    • Krüger R, Kuhn W, Müller T, et al. Ala30Pro mutation in the gene encoding α-synuclein in Parkinson's disease. Nat Genet 1998;18:106-108.
    • (1998) Nat Genet , vol.18 , pp. 106-108
    • Krüger, R.1    Kuhn, W.2    Müller, T.3
  • 9
    • 10744230149 scopus 로고    scopus 로고
    • The new mutation, E46K, of α-synuclein causes Parkinson and Lewy body dementia
    • Zarranz JJ, Alegre J, Gómez-Esteban JC, et al. The new mutation, E46K, of α-synuclein causes Parkinson and Lewy body dementia. Ann Neurol 2004;55:164-173.
    • (2004) Ann Neurol , vol.55 , pp. 164-173
    • Zarranz, J.J.1    Alegre, J.2    Gómez-Esteban, J.C.3
  • 10
    • 84879605541 scopus 로고    scopus 로고
    • α-synuclein p.H50Q, a novel pathogenic mutation for Parkinson's disease
    • Appel-Cresswell S, Vilarino-Guell C, Encarnacion M, et al. α-synuclein p.H50Q, a novel pathogenic mutation for Parkinson's disease. Mov Disord 2013;28:811-813.
    • (2013) Mov Disord , vol.28 , pp. 811-813
    • Appel-Cresswell, S.1    Vilarino-Guell, C.2    Encarnacion, M.3
  • 11
    • 84878405578 scopus 로고    scopus 로고
    • G51D α-synuclein mutation causes a novel parkinsonian-pyramidal syndrome
    • Lesage S, Anheim M, Letournel F, et al. G51D α-synuclein mutation causes a novel parkinsonian-pyramidal syndrome. Ann Neurol 2013;73:459-471.
    • (2013) Ann Neurol , vol.73 , pp. 459-471
    • Lesage, S.1    Anheim, M.2    Letournel, F.3
  • 12
    • 84876226920 scopus 로고    scopus 로고
    • A novel α-synuclein missense mutation in Parkinson disease
    • Proukakis C, Dudzik CG, Brier T, et al. A novel α-synuclein missense mutation in Parkinson disease. Neurology 2013;80:1062-1064.
    • (2013) Neurology , vol.80 , pp. 1062-1064
    • Proukakis, C.1    Dudzik, C.G.2    Brier, T.3
  • 13
    • 4644290985 scopus 로고    scopus 로고
    • α-synuclein locus duplication as a cause of familial Parkinson's disease
    • Chartier-Harlin M-C, Kachergus J, Roumier C, et al. α-synuclein locus duplication as a cause of familial Parkinson's disease. Lancet 364:1167-1169.
    • Lancet , vol.364 , pp. 1167-1169
    • Chartier-Harlin, M.-C.1    Kachergus, J.2    Roumier, C.3
  • 14
    • 58449106639 scopus 로고    scopus 로고
    • α-synuclein gene rearrangements in dominantly inherited parkinsonism: frequency, phenotype, and mechanisms
    • Ibáñez P, Lesage S, Janin S, et al. α-synuclein gene rearrangements in dominantly inherited parkinsonism: frequency, phenotype, and mechanisms. Arch Neurol 2009;66:102-108.
    • (2009) Arch Neurol , vol.66 , pp. 102-108
    • Ibáñez, P.1    Lesage, S.2    Janin, S.3
  • 15
    • 0242300619 scopus 로고    scopus 로고
    • α-Synuclein locus triplication causes Parkinson's disease
    • Singleton AB, Farrer M, Johnson J, et al. α-Synuclein locus triplication causes Parkinson's disease. Science 2003;302:841.
    • (2003) Science , vol.302 , pp. 841
    • Singleton, A.B.1    Farrer, M.2    Johnson, J.3
  • 16
    • 10744227740 scopus 로고    scopus 로고
    • Comparison of kindreds with parkinsonism and α-synuclein genomic multiplications
    • Farrer M, Kachergus J, Forno L, et al. Comparison of kindreds with parkinsonism and α-synuclein genomic multiplications. Ann Neurol 2004;55:174-179.
    • (2004) Ann Neurol , vol.55 , pp. 174-179
    • Farrer, M.1    Kachergus, J.2    Forno, L.3
  • 17
    • 77954969061 scopus 로고    scopus 로고
    • Atypical parkinsonism with apraxia and supranuclear gaze abnormalities in type 1 Gaucher disease: expanding the spectrum: case report and literature review
    • Alonso-Canovas A, Katschnig P, Tucci A, et al. Atypical parkinsonism with apraxia and supranuclear gaze abnormalities in type 1 Gaucher disease: expanding the spectrum: case report and literature review. Mov Disord 2010;25:1506-1509.
    • (2010) Mov Disord , vol.25 , pp. 1506-1509
    • Alonso-Canovas, A.1    Katschnig, P.2    Tucci, A.3
  • 18
    • 0029773625 scopus 로고    scopus 로고
    • Occurrence of Parkinson's syndrome in type I Gaucher disease
    • Neudorfer O, Giladi N, Elstein D, et al. Occurrence of Parkinson's syndrome in type I Gaucher disease. QJM 1996;89:691-694.
    • (1996) QJM , vol.89 , pp. 691-694
    • Neudorfer, O.1    Giladi, N.2    Elstein, D.3
  • 19
    • 0038727936 scopus 로고    scopus 로고
    • Description of Parkinson's disease as a clinical syndrome
    • Fahn S. Description of Parkinson's disease as a clinical syndrome. Ann N Y Acad Sci 2003;991:1-14.
    • (2003) Ann N Y Acad Sci , vol.991 , pp. 1-14
    • Fahn, S.1
  • 20
    • 0028985267 scopus 로고
    • The precursor protein of non-A beta component of Alzheimer's disease amyloid is a presynaptic protein of the central nervous system
    • Iwai A, Masliah E, Yoshimoto M, et al. The precursor protein of non-A beta component of Alzheimer's disease amyloid is a presynaptic protein of the central nervous system. Neuron 1995;14:467-475.
    • (1995) Neuron , vol.14 , pp. 467-475
    • Iwai, A.1    Masliah, E.2    Yoshimoto, M.3
  • 21
    • 0037195109 scopus 로고    scopus 로고
    • Resistance of α-synuclein null mice to the parkinsonian neurotoxin MPTP
    • Dauer W, Kholodilov N, Vila M, et al. Resistance of α-synuclein null mice to the parkinsonian neurotoxin MPTP. Proc Natl Acad Sci U S A 2002;99:14524-14529.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 14524-14529
    • Dauer, W.1    Kholodilov, N.2    Vila, M.3
  • 22
    • 0025943571 scopus 로고
    • The rat brain synucleins: family of proteins transiently associated with neuronal membrane
    • Maroteaux L, Scheller RH. The rat brain synucleins: family of proteins transiently associated with neuronal membrane. Brain Res Mol Brain Res 1991;11:335-343.
    • (1991) Brain Res Mol Brain Res , vol.11 , pp. 335-343
    • Maroteaux, L.1    Scheller, R.H.2
  • 23
    • 3342951965 scopus 로고    scopus 로고
    • Lipid rafts mediate the synaptic localization of α-synuclein
    • Fortin DL, Troyer MD, Nakamura K, et al. Lipid rafts mediate the synaptic localization of α-synuclein. J Neurosci 2004;24:6715-6723.
    • (2004) J Neurosci , vol.24 , pp. 6715-6723
    • Fortin, D.L.1    Troyer, M.D.2    Nakamura, K.3
  • 24
    • 0034280435 scopus 로고    scopus 로고
    • Subcellular localization of wild-type and Parkinson's disease-associated mutant α-synuclein in human and transgenic mouse brain
    • Kahle PJ, Neumann M, Ozmen L, et al. Subcellular localization of wild-type and Parkinson's disease-associated mutant α-synuclein in human and transgenic mouse brain. J Neurosci 2000;20:6365-6373.
    • (2000) J Neurosci , vol.20 , pp. 6365-6373
    • Kahle, P.J.1    Neumann, M.2    Ozmen, L.3
  • 25
    • 0023722437 scopus 로고
    • Synuclein: a neuron-specific protein localized to the nucleus and presynaptic nerve terminal
    • Maroteaux L, Campanelli JT, Scheller RH. Synuclein: a neuron-specific protein localized to the nucleus and presynaptic nerve terminal. J Neurosci 1988;8:2804-2815.
    • (1988) J Neurosci , vol.8 , pp. 2804-2815
    • Maroteaux, L.1    Campanelli, J.T.2    Scheller, R.H.3
  • 26
    • 84887273441 scopus 로고    scopus 로고
    • Assessing the subcellular dynamics of α-synuclein using photoactivation microscopy
    • Gonçalves S, Outeiro TF. Assessing the subcellular dynamics of α-synuclein using photoactivation microscopy. Mol Neurobiol 2013;47:1081-1092.
    • (2013) Mol Neurobiol , vol.47 , pp. 1081-1092
    • Gonçalves, S.1    Outeiro, T.F.2
  • 27
    • 0033724436 scopus 로고    scopus 로고
    • Subcellular localization of α-synuclein in primary neuronal cultures: effect of missense mutations
    • McLean PJ, Ribich S, Hyman BT. Subcellular localization of α-synuclein in primary neuronal cultures: effect of missense mutations. J Neural Transm Suppl 2000;58:53-63.
    • (2000) J Neural Transm Suppl , vol.58 , pp. 53-63
    • McLean, P.J.1    Ribich, S.2    Hyman, B.T.3
  • 28
    • 0037150773 scopus 로고    scopus 로고
    • Immunohistochemical comparison of aa- and beta-synuclein in adult rat central nervous system
    • Mori F, Tanji K, Yoshimoto M, et al. Immunohistochemical comparison of aa- and beta-synuclein in adult rat central nervous system. Brain Res 2002;941:118-126.
    • (2002) Brain Res , vol.941 , pp. 118-126
    • Mori, F.1    Tanji, K.2    Yoshimoto, M.3
  • 29
    • 0038456964 scopus 로고    scopus 로고
    • Nuclear localization of α-synuclein and its interaction with histones
    • Goers J, Manning-Bog AB, McCormack AL, et al. Nuclear localization of α-synuclein and its interaction with histones. Biochemistry 2003;42:8465-8471.
    • (2003) Biochemistry , vol.42 , pp. 8465-8471
    • Goers, J.1    Manning-Bog, A.B.2    McCormack, A.L.3
  • 30
    • 33749583553 scopus 로고    scopus 로고
    • α-synuclein acts in the nucleus to inhibit histone acetylation and promote neurotoxicity
    • Kontopoulos E, Parvin JD, Feany MB. α-synuclein acts in the nucleus to inhibit histone acetylation and promote neurotoxicity. Hum Mol Genet 2006;15:3012-3023.
    • (2006) Hum Mol Genet , vol.15 , pp. 3012-3023
    • Kontopoulos, E.1    Parvin, J.D.2    Feany, M.B.3
  • 31
    • 13444254033 scopus 로고    scopus 로고
    • Subcellular localisation of recombinant aa- and gamma-synuclein
    • Specht CG, Tigaret CM, Rast GF, et al. Subcellular localisation of recombinant aa- and gamma-synuclein. Mol Cell Neurosci 2005;28:326-334.
    • (2005) Mol Cell Neurosci , vol.28 , pp. 326-334
    • Specht, C.G.1    Tigaret, C.M.2    Rast, G.F.3
  • 32
    • 44749085250 scopus 로고    scopus 로고
    • Mitochondrial translocation of α-synuclein is promoted by intracellular acidification
    • Cole NB, Dieuliis D, Leo P, et al. Mitochondrial translocation of α-synuclein is promoted by intracellular acidification. Exp Cell Res 2008;314:2076-2089.
    • (2008) Exp Cell Res , vol.314 , pp. 2076-2089
    • Cole, N.B.1    Dieuliis, D.2    Leo, P.3
  • 33
    • 44049099669 scopus 로고    scopus 로고
    • Mitochondrial import and accumulation of α-synuclein impair complex I in human dopaminergic neuronal cultures and Parkinson disease brain
    • Devi L, Raghavendran V, Prabhu BM, et al. Mitochondrial import and accumulation of α-synuclein impair complex I in human dopaminergic neuronal cultures and Parkinson disease brain. J Biol Chem 2008;283:9089-9100.
    • (2008) J Biol Chem , vol.283 , pp. 9089-9100
    • Devi, L.1    Raghavendran, V.2    Prabhu, B.M.3
  • 34
    • 44649150145 scopus 로고    scopus 로고
    • Mitochondrial localization of α-synuclein protein in α-synuclein overexpressing cells
    • Shavali S, Brown-Borg HM, Ebadi M, Porter J. Mitochondrial localization of α-synuclein protein in α-synuclein overexpressing cells. Neurosci Lett 2008;439:125-128.
    • (2008) Neurosci Lett , vol.439 , pp. 125-128
    • Shavali, S.1    Brown-Borg, H.M.2    Ebadi, M.3    Porter, J.4
  • 35
    • 77958449984 scopus 로고    scopus 로고
    • α-Synuclein: membrane interactions and toxicity in Parkinson's disease
    • Auluck PK, Caraveo G, Lindquist S. α-Synuclein: membrane interactions and toxicity in Parkinson's disease. Annu Rev Cell Dev Biol 2010;26:211-233.
    • (2010) Annu Rev Cell Dev Biol , vol.26 , pp. 211-233
    • Auluck, P.K.1    Caraveo, G.2    Lindquist, S.3
  • 36
    • 82755176258 scopus 로고    scopus 로고
    • Membrane curvature sensing by amphipathic helices: a single liposome study using α-synuclein and annexin B12
    • Jensen MB, Bhatia VK, Jao CC, et al. Membrane curvature sensing by amphipathic helices: a single liposome study using α-synuclein and annexin B12. J Biol Chem 2011;286:42603-42614.
    • (2011) J Biol Chem , vol.286 , pp. 42603-42614
    • Jensen, M.B.1    Bhatia, V.K.2    Jao, C.C.3
  • 37
    • 77958455514 scopus 로고    scopus 로고
    • Effects of curvature and composition on α-synuclein binding to lipid vesicles
    • Middleton ER, Rhoades E. Effects of curvature and composition on α-synuclein binding to lipid vesicles. Biophys J 2010;99:2279-2288.
    • (2010) Biophys J , vol.99 , pp. 2279-2288
    • Middleton, E.R.1    Rhoades, E.2
  • 38
    • 24744432079 scopus 로고    scopus 로고
    • A combinatorial code for the interaction of α-synuclein with membranes
    • Kubo S, Nemani VM, Chalkley RJ, et al. A combinatorial code for the interaction of α-synuclein with membranes. J Biol Chem 2005;280:31664-31672.
    • (2005) J Biol Chem , vol.280 , pp. 31664-31672
    • Kubo, S.1    Nemani, V.M.2    Chalkley, R.J.3
  • 39
    • 77951239770 scopus 로고    scopus 로고
    • The transgenic overexpression of αα-synuclein and not its related pathology associates with complex I inhibition
    • Loeb V, Yakunin E, Saada A, Sharon R. The transgenic overexpression of αα-synuclein and not its related pathology associates with complex I inhibition. J Biol Chem 2010;285:7334-7343.
    • (2010) J Biol Chem , vol.285 , pp. 7334-7343
    • Loeb, V.1    Yakunin, E.2    Saada, A.3    Sharon, R.4
  • 40
    • 78049383132 scopus 로고    scopus 로고
    • Mitochondrial α-synuclein accumulation impairs complex I function in dopaminergic neurons and results in increased mitophagy in vivo
    • Chinta SJ, Mallajosyula JK, Rane A, Andersen JK. Mitochondrial α-synuclein accumulation impairs complex I function in dopaminergic neurons and results in increased mitophagy in vivo. Neurosci Lett 2010;486:235-239.
    • (2010) Neurosci Lett , vol.486 , pp. 235-239
    • Chinta, S.J.1    Mallajosyula, J.K.2    Rane, A.3    Andersen, J.K.4
  • 41
    • 68949218403 scopus 로고    scopus 로고
    • Leucine-rich repeat kinase 2 phosphorylates brain tubulin-beta isoforms and modulates microtubule stability: a point of convergence in parkinsonian neurodegeneration?
    • Gillardon F. Leucine-rich repeat kinase 2 phosphorylates brain tubulin-beta isoforms and modulates microtubule stability: a point of convergence in parkinsonian neurodegeneration? J Neurochem 2009;110:1514-1522.
    • (2009) J Neurochem , vol.110 , pp. 1514-1522
    • Gillardon, F.1
  • 42
    • 33845656077 scopus 로고    scopus 로고
    • Impairment of microtubule-dependent trafficking by overexpression of α-synuclein
    • Lee H-J, Khoshaghideh F, Lee S, Lee S-J. Impairment of microtubule-dependent trafficking by overexpression of α-synuclein. Eur J Neurosci 2006;24:3153-3162.
    • (2006) Eur J Neurosci , vol.24 , pp. 3153-3162
    • Lee, H.-J.1    Khoshaghideh, F.2    Lee, S.3    Lee, S.-J.4
  • 43
    • 64549112144 scopus 로고    scopus 로고
    • Pink1 forms a multiprotein complex with Miro and Milton, linking Pink1 function to mitochondrial trafficking
    • Weihofen A, Thomas KJ, Ostaszewski BL, et al. Pink1 forms a multiprotein complex with Miro and Milton, linking Pink1 function to mitochondrial trafficking. Biochemistry 2009;48:2045-2052.
    • (2009) Biochemistry , vol.48 , pp. 2045-2052
    • Weihofen, A.1    Thomas, K.J.2    Ostaszewski, B.L.3
  • 44
    • 20444451210 scopus 로고    scopus 로고
    • Parkin stabilizes microtubules through strong binding mediated by three independent domains
    • Yang F, Jiang Q, Zhao J, et al. Parkin stabilizes microtubules through strong binding mediated by three independent domains. J Biol Chem 2005;280:17154-17162.
    • (2005) J Biol Chem , vol.280 , pp. 17154-17162
    • Yang, F.1    Jiang, Q.2    Zhao, J.3
  • 45
    • 34347359673 scopus 로고    scopus 로고
    • Rejuvenation” protects neurons in mouse models of Parkinson's disease
    • Chan CS, Guzman JN, Ilijic E, et al. “Rejuvenation” protects neurons in mouse models of Parkinson's disease. Nature 2007;447:1081-1086.
    • (2007) Nature , vol.447 , pp. 1081-1086
    • Chan, C.S.1    Guzman, J.N.2    Ilijic, E.3
  • 46
    • 65249180086 scopus 로고    scopus 로고
    • Interplay between cytosolic dopamine, calcium, and α-synuclein causes selective death of substantia nigra neurons
    • Mosharov E V, Larsen KE, Kanter E, et al. Interplay between cytosolic dopamine, calcium, and α-synuclein causes selective death of substantia nigra neurons. Neuron 2009;62:218-229.
    • (2009) Neuron , vol.62 , pp. 218-229
    • Mosharov, E.V.1    Larsen, K.E.2    Kanter, E.3
  • 47
    • 37049004489 scopus 로고    scopus 로고
    • Mitochondria in the aetiology and pathogenesis of Parkinson's disease
    • Schapira AH V. Mitochondria in the aetiology and pathogenesis of Parkinson's disease. Lancet Neurol 2008;7:97-109.
    • (2008) Lancet Neurol , vol.7 , pp. 97-109
    • Schapira, A.H.V.1
  • 48
    • 77955346228 scopus 로고    scopus 로고
    • Identifying PD-causing genes and genetic susceptibility factors: current approaches and future prospects
    • Gasser T. Identifying PD-causing genes and genetic susceptibility factors: current approaches and future prospects. Prog Brain Res 2010;183:3-20.
    • (2010) Prog Brain Res , vol.183 , pp. 3-20
    • Gasser, T.1
  • 49
    • 78649866553 scopus 로고    scopus 로고
    • Oxidant stress evoked by pacemaking in dopaminergic neurons is attenuated by DJ-1
    • Guzman JN, Sanchez-Padilla J, Wokosin D, et al. Oxidant stress evoked by pacemaking in dopaminergic neurons is attenuated by DJ-1. Nature 2010;468:696-700.
    • (2010) Nature , vol.468 , pp. 696-700
    • Guzman, J.N.1    Sanchez-Padilla, J.2    Wokosin, D.3
  • 50
    • 77955364853 scopus 로고    scopus 로고
    • The impact of genetic research on our understanding of Parkinson's disease
    • Martin I, Dawson VL, Dawson TM. The impact of genetic research on our understanding of Parkinson's disease. Prog Brain Res 2010;183:21-41.
    • (2010) Prog Brain Res , vol.183 , pp. 21-41
    • Martin, I.1    Dawson, V.L.2    Dawson, T.M.3
  • 51
    • 79952199282 scopus 로고    scopus 로고
    • Modeling clinical features of neurodegeneration
    • Obeso JA. Modeling clinical features of neurodegeneration. Nat Med 2010;16:1372.
    • (2010) Nat Med , vol.16 , pp. 1372
    • Obeso, J.A.1
  • 52
    • 77549084979 scopus 로고    scopus 로고
    • Calcium, cellular aging, and selective neuronal vulnerability in Parkinson's disease
    • Surmeier DJ, Guzman JN, Sanchez-Padilla J. Calcium, cellular aging, and selective neuronal vulnerability in Parkinson's disease. Cell Calcium 2010;47:175-182.
    • (2010) Cell Calcium , vol.47 , pp. 175-182
    • Surmeier, D.J.1    Guzman, J.N.2    Sanchez-Padilla, J.3
  • 54
    • 79959305691 scopus 로고    scopus 로고
    • Mitochondria: the next (neurode)generation
    • Schon EA, Przedborski S. Mitochondria: the next (neurode)generation. Neuron 2011;70:1033-1053.
    • (2011) Neuron , vol.70 , pp. 1033-1053
    • Schon, E.A.1    Przedborski, S.2
  • 55
    • 84890115517 scopus 로고    scopus 로고
    • Isogenic human iPSC Parkinson's model shows nitrosative stress-induced dysfunction in MEF2-PGC1α transcription
    • Ryan SD, Dolatabadi N, Chan SF, et al. Isogenic human iPSC Parkinson's model shows nitrosative stress-induced dysfunction in MEF2-PGC1α transcription. Cell 2013;155:1351-1364.
    • (2013) Cell , vol.155 , pp. 1351-1364
    • Ryan, S.D.1    Dolatabadi, N.2    Chan, S.F.3
  • 56
    • 34748826792 scopus 로고    scopus 로고
    • Localization of α-synuclein to mitochondria within midbrain of mice
    • Li W-W, Yang R, Guo J-C, et al. Localization of α-synuclein to mitochondria within midbrain of mice. Neuroreport 2007;18:1543-1546.
    • (2007) Neuroreport , vol.18 , pp. 1543-1546
    • Li, W.-W.1    Yang, R.2    Guo, J.-C.3
  • 57
    • 42449095464 scopus 로고    scopus 로고
    • Mitochondrial association of α-synuclein causes oxidative stress
    • Parihar MS, Parihar A, Fujita M, et al. Mitochondrial association of α-synuclein causes oxidative stress. Cell Mol Life Sci 2008;65:1272-1284.
    • (2008) Cell Mol Life Sci , vol.65 , pp. 1272-1284
    • Parihar, M.S.1    Parihar, A.2    Fujita, M.3
  • 58
    • 0037092442 scopus 로고    scopus 로고
    • A role for a-synuclein in the regulation of dopamine biosynthesis
    • Perez RG, Waymire JC, Lin E, et al. A role for a-synuclein in the regulation of dopamine biosynthesis. J Neurosci 2002;22:3090-3099.
    • (2002) J Neurosci , vol.22 , pp. 3090-3099
    • Perez, R.G.1    Waymire, J.C.2    Lin, E.3
  • 59
    • 66449090816 scopus 로고    scopus 로고
    • Mitochondria do not contain lipid rafts, and lipid rafts do not contain mitochondrial proteins
    • Zheng YZ, Berg KB, Foster LJ. Mitochondria do not contain lipid rafts, and lipid rafts do not contain mitochondrial proteins. J Lipid Res 2009;50:988-998.
    • (2009) J Lipid Res , vol.50 , pp. 988-998
    • Zheng, Y.Z.1    Berg, K.B.2    Foster, L.J.3
  • 61
    • 77950284301 scopus 로고    scopus 로고
    • Detergent-resistant microdomains determine the localization of sigma-1 receptors to the endoplasmic reticulum-mitochondria junction
    • Hayashi T, Fujimoto M. Detergent-resistant microdomains determine the localization of sigma-1 receptors to the endoplasmic reticulum-mitochondria junction. Mol Pharmacol 2010;77:517-528.
    • (2010) Mol Pharmacol , vol.77 , pp. 517-528
    • Hayashi, T.1    Fujimoto, M.2
  • 62
    • 84868524156 scopus 로고    scopus 로고
    • Upregulated function of mitochondria-associated ER membranes in Alzheimer disease
    • Area-Gomez E, Del Carmen Lara Castillo M, Tambini MD, et al. Upregulated function of mitochondria-associated ER membranes in Alzheimer disease. EMBO J 2012;31:4106-4123.
    • (2012) EMBO J , vol.31 , pp. 4106-4123
    • Area-Gomez, E.1    Del Carmen Lara Castillo, M.2    Tambini, M.D.3
  • 63
    • 84855810521 scopus 로고    scopus 로고
    • The role of cholesterol in the association of endoplasmic reticulum membranes with mitochondria
    • Fujimoto M, Hayashi T, Su T-P. The role of cholesterol in the association of endoplasmic reticulum membranes with mitochondria. Biochem Biophys Res Commun 2012;417:635-639.
    • (2012) Biochem Biophys Res Commun , vol.417 , pp. 635-639
    • Fujimoto, M.1    Hayashi, T.2    Su, T.-P.3
  • 64
    • 79551703425 scopus 로고    scopus 로고
    • The human cytomegalovirus protein UL37 exon 1 associates with internal lipid rafts
    • Williamson CD, Zhang A, Colberg-Poley AM. The human cytomegalovirus protein UL37 exon 1 associates with internal lipid rafts. J Virol 2011;85:2100-2111.
    • (2011) J Virol , vol.85 , pp. 2100-2111
    • Williamson, C.D.1    Zhang, A.2    Colberg-Poley, A.M.3
  • 65
    • 33644847375 scopus 로고    scopus 로고
    • 2+: molecular determinants and functional consequences
    • 2+: molecular determinants and functional consequences. Physiol Rev 2006;86:369-408.
    • (2006) Physiol Rev , vol.86 , pp. 369-408
    • Rizzuto, R.1    Pozzan, T.2
  • 66
    • 67650747650 scopus 로고    scopus 로고
    • Genetic and biochemical analysis of non-vesicular lipid traffic
    • Voelker DR. Genetic and biochemical analysis of non-vesicular lipid traffic. Annu Rev Biochem 2009;78:827-856.
    • (2009) Annu Rev Biochem , vol.78 , pp. 827-856
    • Voelker, D.R.1
  • 67
    • 68649116755 scopus 로고    scopus 로고
    • SR/ER-mitochondrial local communication: calcium and ROS
    • Csordás G, Hajnóczky G. SR/ER-mitochondrial local communication: calcium and ROS. Biochim Biophys Acta 2009;1787:1352-1362.
    • (2009) Biochim Biophys Acta , vol.1787 , pp. 1352-1362
    • Csordás, G.1    Hajnóczky, G.2
  • 68
    • 77953725586 scopus 로고    scopus 로고
    • Oxidative protein folding in the endoplasmic reticulum: tight links to the mitochondria-associated membrane (MAM)
    • Simmen T, Lynes EM, Gesson K, Thomas G. Oxidative protein folding in the endoplasmic reticulum: tight links to the mitochondria-associated membrane (MAM). Biochim Biophys Acta 2010;1798:1465-1473.
    • (2010) Biochim Biophys Acta , vol.1798 , pp. 1465-1473
    • Simmen, T.1    Lynes, E.M.2    Gesson, K.3    Thomas, G.4
  • 69
    • 80051770868 scopus 로고    scopus 로고
    • The role of PML in the control of apoptotic cell fate: a new key player at ER-mitochondria sites
    • Pinton P, Giorgi C, Pandolfi PP. The role of PML in the control of apoptotic cell fate: a new key player at ER-mitochondria sites. Cell Death Differ 2011;18:1450-1456.
    • (2011) Cell Death Differ , vol.18 , pp. 1450-1456
    • Pinton, P.1    Giorgi, C.2    Pandolfi, P.P.3
  • 70
    • 80053175932 scopus 로고    scopus 로고
    • Calcium signaling around mitochondria associated membranes (MAMs)
    • Patergnani S, Suski JM, Agnoletto C, et al. Calcium signaling around mitochondria associated membranes (MAMs). Cell Commun Signal 2011;9:19.
    • (2011) Cell Commun Signal , vol.9 , pp. 19
    • Patergnani, S.1    Suski, J.M.2    Agnoletto, C.3
  • 71
    • 33845656077 scopus 로고    scopus 로고
    • Impairment of microtubule-dependent trafficking by overexpression of a-synuclein
    • Lee H-J, Khoshaghideh F, Lee S, Lee S-J. Impairment of microtubule-dependent trafficking by overexpression of a-synuclein. Eur J Neurosci 2006;24:3153-3162.
    • (2006) Eur J Neurosci , vol.24 , pp. 3153-3162
    • Lee, H.-J.1    Khoshaghideh, F.2    Lee, S.3    Lee, S.-J.4
  • 72
    • 64549112144 scopus 로고    scopus 로고
    • Pink1 forms a multiprotein complex with Miro and Milton, linking Pink1 function to mitochondrial trafficking
    • Weihofen A, Thomas KJ, Ostaszewski BL, et al. Pink1 forms a multiprotein complex with Miro and Milton, linking Pink1 function to mitochondrial trafficking. Biochemistry 2009;48:2045-2052.
    • (2009) Biochemistry , vol.48 , pp. 2045-2052
    • Weihofen, A.1    Thomas, K.J.2    Ostaszewski, B.L.3
  • 74
    • 84877337663 scopus 로고    scopus 로고
    • Modulation of the endoplasmic reticulum-mitochondria interface in Alzheimer's disease and related models
    • Hedskog L, Pinho CM, Filadi R, et al. Modulation of the endoplasmic reticulum-mitochondria interface in Alzheimer's disease and related models. Proc Natl Acad Sci U S A 2013;110:7916-7921.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 7916-7921
    • Hedskog, L.1    Pinho, C.M.2    Filadi, R.3
  • 75
    • 84901925681 scopus 로고    scopus 로고
    • ER-mitochondria associations are regulated by the VAPB-PTPIP51 interaction and are disrupted by amyotrophic lateral sclerosis/FTD-associated TDP-43
    • Stoica R, De Vos KJ, Paillusson S, et al. ER-mitochondria associations are regulated by the VAPB-PTPIP51 interaction and are disrupted by amyotrophic lateral sclerosis/FTD-associated TDP-43. Nat Commun 2014;5:3996.
    • (2014) Nat Commun , vol.5 , pp. 3996
    • Stoica, R.1    De Vos, K.J.2    Paillusson, S.3
  • 76
    • 84861554724 scopus 로고    scopus 로고
    • α-Synuclein controls mitochondrial calcium homeostasis by enhancing endoplasmic reticulum-mitochondria interactions
    • Calì T, Ottolini D, Negro A, Brini M. α-Synuclein controls mitochondrial calcium homeostasis by enhancing endoplasmic reticulum-mitochondria interactions. J Biol Chem 2012;287:17914-17929.
    • (2012) J Biol Chem , vol.287 , pp. 17914-17929
    • Calì, T.1    Ottolini, D.2    Negro, A.3    Brini, M.4
  • 77
    • 73649098791 scopus 로고    scopus 로고
    • Presenilins are enriched in endoplasmic reticulum membranes associated with mitochondria
    • Area-Gomez E, de Groof AJC, Boldogh I, et al. Presenilins are enriched in endoplasmic reticulum membranes associated with mitochondria. Am J Pathol 2009;175:1810-1816.
    • (2009) Am J Pathol , vol.175 , pp. 1810-1816
    • Area-Gomez, E.1    de Groof, A.J.C.2    Boldogh, I.3
  • 78
    • 79959362111 scopus 로고    scopus 로고
    • Structural and morphological characterization of aggregated species of α-synuclein induced by docosahexaenoic acid
    • De Franceschi G, Frare E, Pivato M, et al. Structural and morphological characterization of aggregated species of α-synuclein induced by docosahexaenoic acid. J Biol Chem 2011;286:22262-22274.
    • (2011) J Biol Chem , vol.286 , pp. 22262-22274
    • De Franceschi, G.1    Frare, E.2    Pivato, M.3
  • 79
    • 79954534373 scopus 로고    scopus 로고
    • Molecular basis for the glycosphingolipid-binding specificity of α-synuclein: key role of tyrosine 39 in membrane insertion
    • Fantini J, Yahi N. Molecular basis for the glycosphingolipid-binding specificity of α-synuclein: key role of tyrosine 39 in membrane insertion. J Mol Biol 2011;408:654-669.
    • (2011) J Mol Biol , vol.408 , pp. 654-669
    • Fantini, J.1    Yahi, N.2
  • 80
    • 79960351124 scopus 로고    scopus 로고
    • Caveolin-1 interacts with a-synuclein and mediates toxic actions of cellular a-synuclein overexpression
    • Madeira A, Yang J, Zhang X, et al. Caveolin-1 interacts with a-synuclein and mediates toxic actions of cellular a-synuclein overexpression. Neurochem Int 2011;59:280-289.
    • (2011) Neurochem Int , vol.59 , pp. 280-289
    • Madeira, A.1    Yang, J.2    Zhang, X.3
  • 81
    • 50849130565 scopus 로고    scopus 로고
    • Phosphorylation, lipid raft interaction and traffic of a-synuclein in a yeast model for Parkinson
    • Zabrocki P, Bastiaens I, Delay C, et al. Phosphorylation, lipid raft interaction and traffic of a-synuclein in a yeast model for Parkinson. Biochim Biophys Acta 2008;1783:1767-1780.
    • (2008) Biochim Biophys Acta , vol.1783 , pp. 1767-1780
    • Zabrocki, P.1    Bastiaens, I.2    Delay, C.3
  • 82
    • 41749101449 scopus 로고    scopus 로고
    • Lipid rafts association of synaptotagmin I on synaptic vesicles
    • Lv J-H, He L, Sui S-F. Lipid rafts association of synaptotagmin I on synaptic vesicles. Biochem Biokhimiia 2008;73:283-288.
    • (2008) Biochem Biokhimiia , vol.73 , pp. 283-288
    • Lv, J.-H.1    He, L.2    Sui, S.-F.3
  • 83
    • 84857654809 scopus 로고    scopus 로고
    • Development of the sigma-1 receptor in C-terminals of motoneurons and colocalization with the N,N'-dimethyltryptamine forming enzyme, indole-N-methyl transferase
    • Mavlyutov TA, Epstein ML, Liu P, et al. Development of the sigma-1 receptor in C-terminals of motoneurons and colocalization with the N,N'-dimethyltryptamine forming enzyme, indole-N-methyl transferase. Neuroscience 2012;206:60-68.
    • (2012) Neuroscience , vol.206 , pp. 60-68
    • Mavlyutov, T.A.1    Epstein, M.L.2    Liu, P.3
  • 84
    • 35549006797 scopus 로고    scopus 로고
    • Sigma-1 receptor chaperones at the ER-mitochondrion interface regulate Ca(2+) signaling and cell survival
    • Hayashi T, Su T-P. Sigma-1 receptor chaperones at the ER-mitochondrion interface regulate Ca(2+) signaling and cell survival. Cell 2007;131:596-610.
    • (2007) Cell , vol.131 , pp. 596-610
    • Hayashi, T.1    Su, T.-P.2
  • 85
    • 0032540327 scopus 로고    scopus 로고
    • Stabilization of a-synuclein secondary structure upon binding to synthetic membranes
    • Davidson WS, Jonas A, Clayton DF, George JM. Stabilization of a-synuclein secondary structure upon binding to synthetic membranes J Biol Chem 1998;273:9443-9449.
    • (1998) J Biol Chem , vol.273 , pp. 9443-9449
    • Davidson, W.S.1    Jonas, A.2    Clayton, D.F.3    George, J.M.4
  • 86
    • 79957974579 scopus 로고    scopus 로고
    • Direct membrane association drives mitochondrial fission by the Parkinson Disease-associated protein a-synuclein
    • Nakamura K, Nemani VM, Azarbal F, et al. Direct membrane association drives mitochondrial fission by the Parkinson Disease-associated protein a-synuclein. J Biol Chem 2011;286:20710-20726.
    • (2011) J Biol Chem , vol.286 , pp. 20710-20726
    • Nakamura, K.1    Nemani, V.M.2    Azarbal, F.3
  • 87
    • 21744445061 scopus 로고    scopus 로고
    • Bridging gaps in phospholipid transport
    • Voelker DR. Bridging gaps in phospholipid transport. Trends Biochem Sci 2005;30:396-404.
    • (2005) Trends Biochem Sci , vol.30 , pp. 396-404
    • Voelker, D.R.1
  • 88
    • 84891410019 scopus 로고    scopus 로고
    • α-Synuclein is localized to mitochondria-associated ER membranes
    • Guardia-Laguarta C, Area-Gomez E, Rüb C, et al. α-Synuclein is localized to mitochondria-associated ER membranes. J Neurosci 2014;34:249-259.
    • (2014) J Neurosci , vol.34 , pp. 249-259
    • Guardia-Laguarta, C.1    Area-Gomez, E.2    Rüb, C.3
  • 89
    • 84891410019 scopus 로고    scopus 로고
    • α-Synuclein is localized to mitochondria-associated ER membranes
    • Guardia-Laguarta C, Area-Gomez E, Rüb C, et al. α-Synuclein is localized to mitochondria-associated ER membranes. J Neurosci 2014;34:249-259.
    • (2014) J Neurosci , vol.34 , pp. 249-259
    • Guardia-Laguarta, C.1    Area-Gomez, E.2    Rüb, C.3
  • 90
    • 27544504836 scopus 로고    scopus 로고
    • Regulatory mechanism of tyrosine hydroxylase activity
    • Fujisawa H, Okuno S. Regulatory mechanism of tyrosine hydroxylase activity. Biochem Biophys Res Commun 2005;338:271-276.
    • (2005) Biochem Biophys Res Commun , vol.338 , pp. 271-276
    • Fujisawa, H.1    Okuno, S.2
  • 91
    • 9744239461 scopus 로고    scopus 로고
    • Tyrosine hydroxylase phosphorylation: regulation and consequences
    • Dunkley PR, Bobrovskaya L, Graham ME, et al. Tyrosine hydroxylase phosphorylation: regulation and consequences. J Neurochem 2004;91:1025-1043.
    • (2004) J Neurochem , vol.91 , pp. 1025-1043
    • Dunkley, P.R.1    Bobrovskaya, L.2    Graham, M.E.3
  • 92
    • 0023025693 scopus 로고
    • Identification of four phosphorylation sites in the N-terminal region of tyrosine hydroxylase
    • Campbell DG, Hardie DG, Vulliet PR. Identification of four phosphorylation sites in the N-terminal region of tyrosine hydroxylase. J Biol Chem 1986;261:10489-10492.
    • (1986) J Biol Chem , vol.261 , pp. 10489-10492
    • Campbell, D.G.1    Hardie, D.G.2    Vulliet, P.R.3
  • 93
    • 0023644815 scopus 로고
    • Rat pheochromocytoma tyrosine hydroxylase is phosphorylated on serine 40 by an associated protein kinase
    • Pigeon D, Ferrara P, Gros F, Thibault J. Rat pheochromocytoma tyrosine hydroxylase is phosphorylated on serine 40 by an associated protein kinase. J Biol Chem 1987;262:6155-6158.
    • (1987) J Biol Chem , vol.262 , pp. 6155-6158
    • Pigeon, D.1    Ferrara, P.2    Gros, F.3    Thibault, J.4
  • 94
    • 4143079145 scopus 로고    scopus 로고
    • Phosphorylation of Ser19 increases both Ser40 phosphorylation and enzyme activity of tyrosine hydroxylase in intact cells
    • Bobrovskaya L, Dunkley PR, Dickson PW. Phosphorylation of Ser19 increases both Ser40 phosphorylation and enzyme activity of tyrosine hydroxylase in intact cells. J Neurochem 2004;90:857-864.
    • (2004) J Neurochem , vol.90 , pp. 857-864
    • Bobrovskaya, L.1    Dunkley, P.R.2    Dickson, P.W.3
  • 95
    • 0027976186 scopus 로고
    • Dephosphorylation of tyrosine hydroxylase by brain protein phosphatases: a predominant role for type 2A
    • Berresheim U, Kuhn DM. Dephosphorylation of tyrosine hydroxylase by brain protein phosphatases: a predominant role for type 2A. Brain Res 1994;637:273-276.
    • (1994) Brain Res , vol.637 , pp. 273-276
    • Berresheim, U.1    Kuhn, D.M.2
  • 96
    • 0024309434 scopus 로고
    • Identification of protein phosphatase 2A as the major tyrosine hydroxylase phosphatase in adrenal medulla and corpus striatum: evidence from the effects of okadaic acid
    • Haavik J, Schelling DL, Campbell DG, et al. Identification of protein phosphatase 2A as the major tyrosine hydroxylase phosphatase in adrenal medulla and corpus striatum: evidence from the effects of okadaic acid. FEBS Lett 1989;251:36-42.
    • (1989) FEBS Lett , vol.251 , pp. 36-42
    • Haavik, J.1    Schelling, D.L.2    Campbell, D.G.3
  • 97
    • 0036209128 scopus 로고    scopus 로고
    • Tyrosine hydroxylase dephosphorylation by protein phosphatase 2A in bovine adrenal chromaffin cells
    • Leal RB, Sim ATR, Gonçalves CAS, Dunkley PR. Tyrosine hydroxylase dephosphorylation by protein phosphatase 2A in bovine adrenal chromaffin cells. Neurochem Res 2002;27:207-213.
    • (2002) Neurochem Res , vol.27 , pp. 207-213
    • Leal, R.B.1    Sim, A.T.R.2    Gonçalves, C.A.S.3    Dunkley, P.R.4
  • 98
    • 33846979780 scopus 로고    scopus 로고
    • Differential expression of the B'beta regulatory subunit of protein phosphatase 2A modulates tyrosine hydroxylase phosphorylation and catecholamine synthesis
    • Saraf A, Virshup DM, Strack S. Differential expression of the B'beta regulatory subunit of protein phosphatase 2A modulates tyrosine hydroxylase phosphorylation and catecholamine synthesis. J Biol Chem 2007;282:573-580.
    • (2007) J Biol Chem , vol.282 , pp. 573-580
    • Saraf, A.1    Virshup, D.M.2    Strack, S.3
  • 99
    • 79952449396 scopus 로고    scopus 로고
    • Tyrosine hydroxylase and regulation of dopamine synthesis
    • Daubner SC, Le T, Wang S. Tyrosine hydroxylase and regulation of dopamine synthesis. Arch Biochem Biophys 2011;508:1-12.
    • (2011) Arch Biochem Biophys , vol.508 , pp. 1-12
    • Daubner, S.C.1    Le, T.2    Wang, S.3
  • 100
    • 2942552470 scopus 로고    scopus 로고
    • Unlocking the code of 14-3-3
    • Dougherty MK, Morrison DK. Unlocking the code of 14-3-3. J Cell Sci 2004;117:1875-1884.
    • (2004) J Cell Sci , vol.117 , pp. 1875-1884
    • Dougherty, M.K.1    Morrison, D.K.2
  • 101
  • 102
    • 84870039698 scopus 로고    scopus 로고
    • The peripheral binding of 14-3-3γ to membranes involves isoform-specific histidine residues
    • Bustad HJ, Skjaerven L, Ying M, et al. The peripheral binding of 14-3-3γ to membranes involves isoform-specific histidine residues. PLoS One 2012;7:e49671.
    • (2012) PLoS One , vol.7
    • Bustad, H.J.1    Skjaerven, L.2    Ying, M.3
  • 103
    • 84905265912 scopus 로고    scopus 로고
    • Phosphorylation dependence and stoichiometry of the complex formed by tyrosine hydroxylase and 14-3-3γ
    • Kleppe R, Rosati S, Jorge-Finnigan A, et al. Phosphorylation dependence and stoichiometry of the complex formed by tyrosine hydroxylase and 14-3-3γ. Mol Cell Proteomics 2014;13:2017-2030.
    • (2014) Mol Cell Proteomics , vol.13 , pp. 2017-2030
    • Kleppe, R.1    Rosati, S.2    Jorge-Finnigan, A.3
  • 104
    • 84908538422 scopus 로고    scopus 로고
    • Dissection of binding between a phosphorylated tyrosine hydroxylase peptide and 14-3-3?: A complex story elucidated by NMR
    • Hritz J, Byeon I-JL, Krzysiak T, et al. Dissection of binding between a phosphorylated tyrosine hydroxylase peptide and 14-3-3?: A complex story elucidated by NMR. Biophys J 2014;107:2185-2194.
    • (2014) Biophys J , vol.107 , pp. 2185-2194
    • Hritz, J.1    Byeon, I.-J.L.2    Krzysiak, T.3
  • 105
    • 0035019161 scopus 로고    scopus 로고
    • Interaction of phosphorylated tyrosine hydroxylase with 14-3-3 proteins: evidence for a phosphoserine 40-dependent association
    • Kleppe R, Toska K, Haavik J. Interaction of phosphorylated tyrosine hydroxylase with 14-3-3 proteins: evidence for a phosphoserine 40-dependent association. J Neurochem 2001;77:1097-1107.
    • (2001) J Neurochem , vol.77 , pp. 1097-1107
    • Kleppe, R.1    Toska, K.2    Haavik, J.3
  • 106
    • 38949162984 scopus 로고    scopus 로고
    • The 14-3-3 protein affects the conformation of the regulatory domain of human tyrosine hydroxylase
    • Obsilova V, Nedbalkova E, Silhan J, et al. The 14-3-3 protein affects the conformation of the regulatory domain of human tyrosine hydroxylase. Biochemistry 2008;47:1768-1777.
    • (2008) Biochemistry , vol.47 , pp. 1768-1777
    • Obsilova, V.1    Nedbalkova, E.2    Silhan, J.3
  • 107
    • 67649804671 scopus 로고    scopus 로고
    • 14-3-3Zeta contributes to tyrosine hydroxylase activity in MN9D cells: localization of dopamine regulatory proteins to mitochondria
    • Wang J, Lou H, Pedersen CJ, et al. 14-3-3Zeta contributes to tyrosine hydroxylase activity in MN9D cells: localization of dopamine regulatory proteins to mitochondria. J Biol Chem 2009;284:14011-14019.
    • (2009) J Biol Chem , vol.284 , pp. 14011-14019
    • Wang, J.1    Lou, H.2    Pedersen, C.J.3
  • 108
    • 0037127035 scopus 로고    scopus 로고
    • Immunolocalisation of 14-3-3 isoforms in normal and scrapie-infected murine brain
    • Baxter HC, Liu W-G, Forster JL, et al. Immunolocalisation of 14-3-3 isoforms in normal and scrapie-infected murine brain. Neuroscience 2002;109:5-14.
    • (2002) Neuroscience , vol.109 , pp. 5-14
    • Baxter, H.C.1    Liu, W.-G.2    Forster, J.L.3
  • 109
    • 33749570292 scopus 로고    scopus 로고
    • Phosphorylation of Ser-129 is the dominant pathological modification of a-synuclein in familial and sporadic Lewy body disease
    • Anderson JP, Walker DE, Goldstein JM, et al. Phosphorylation of Ser-129 is the dominant pathological modification of a-synuclein in familial and sporadic Lewy body disease. J Biol Chem 2006;281:29739-29752.
    • (2006) J Biol Chem , vol.281 , pp. 29739-29752
    • Anderson, J.P.1    Walker, D.E.2    Goldstein, J.M.3
  • 110
    • 0036174010 scopus 로고    scopus 로고
    • a-Synuclein is phosphorylated in synucleinopathy lesions
    • Fujiwara H, Hasegawa M, Dohmae N, et al. a-Synuclein is phosphorylated in synucleinopathy lesions. Nat Cell Biol 2002;4:160-164.
    • (2002) Nat Cell Biol , vol.4 , pp. 160-164
    • Fujiwara, H.1    Hasegawa, M.2    Dohmae, N.3
  • 111
    • 84887510168 scopus 로고    scopus 로고
    • In vivo modulation of polo-like kinases supports a key role for PLK2 in Ser129 α-synuclein phosphorylation in mouse brain
    • Bergeron M, Motter R, Tanaka P, et al. In vivo modulation of polo-like kinases supports a key role for PLK2 in Ser129 α-synuclein phosphorylation in mouse brain. Neuroscience 2014;256:72-82.
    • (2014) Neuroscience , vol.256 , pp. 72-82
    • Bergeron, M.1    Motter, R.2    Tanaka, P.3
  • 112
    • 84878682977 scopus 로고    scopus 로고
    • Serine 129 phosphorylation of membrane-associated α-synuclein modulates dopamine transporter function in a G protein-coupled receptor kinase-dependent manner
    • S1-S3
    • Hara S, Arawaka S, Sato H, et al. Serine 129 phosphorylation of membrane-associated α-synuclein modulates dopamine transporter function in a G protein-coupled receptor kinase-dependent manner. Mol Biol Cell 2013;24:1649-1660, S1-S3.
    • (2013) Mol Biol Cell , vol.24 , pp. 1649-1660
    • Hara, S.1    Arawaka, S.2    Sato, H.3
  • 113
    • 81255188869 scopus 로고    scopus 로고
    • Authentically phosphorylated α-synuclein at Ser129 accelerates neurodegeneration in a rat model of familial Parkinson's disease
    • Sato H, Arawaka S, Hara S, et al. Authentically phosphorylated α-synuclein at Ser129 accelerates neurodegeneration in a rat model of familial Parkinson's disease. J Neurosci 2011;31:16884-16894.
    • (2011) J Neurosci , vol.31 , pp. 16884-16894
    • Sato, H.1    Arawaka, S.2    Hara, S.3
  • 114
    • 79956317900 scopus 로고    scopus 로고
    • Enhanced phosphatase activity attenuates α-synucleinopathy in a mouse model
    • Lee K-W, Chen W, Junn E, et al. Enhanced phosphatase activity attenuates α-synucleinopathy in a mouse model. J Neurosci 2011;31:6963-6971.
    • (2011) J Neurosci , vol.31 , pp. 6963-6971
    • Lee, K.-W.1    Chen, W.2    Junn, E.3
  • 115
    • 24344470188 scopus 로고    scopus 로고
    • A-synuclein activation of protein phosphatase 2A reduces tyrosine hydroxylase phosphorylation in dopaminergic cells
    • Peng X, Peng XM, Tehranian R, et al. A-synuclein activation of protein phosphatase 2A reduces tyrosine hydroxylase phosphorylation in dopaminergic cells. J Cell Sci 2005;118:3523-3530.
    • (2005) J Cell Sci , vol.118 , pp. 3523-3530
    • Peng, X.1    Peng, X.M.2    Tehranian, R.3
  • 116
    • 0033565874 scopus 로고    scopus 로고
    • a-Synuclein shares physical and functional homology with 14-3-3 proteins
    • Ostrerova N, Petrucelli L, Farrer M, et al. a-Synuclein shares physical and functional homology with 14-3-3 proteins. J Neurosci 1999;19:5782-5791.
    • (1999) J Neurosci , vol.19 , pp. 5782-5791
    • Ostrerova, N.1    Petrucelli, L.2    Farrer, M.3
  • 117
    • 77952915653 scopus 로고    scopus 로고
    • Serine 129 phosphorylation reduces the ability of a-synuclein to regulate tyrosine hydroxylase and protein phosphatase 2A in vitro and in vivo
    • Lou H, Montoya SE, Alerte TNM, et al. Serine 129 phosphorylation reduces the ability of a-synuclein to regulate tyrosine hydroxylase and protein phosphatase 2A in vitro and in vivo. J Biol Chem 2010;285:17648-17661.
    • (2010) J Biol Chem , vol.285 , pp. 17648-17661
    • Lou, H.1    Montoya, S.E.2    Alerte, T.N.M.3
  • 118
    • 78649888254 scopus 로고    scopus 로고
    • Phosphorylation of α-synuclein upregulates tyrosine hydroxylase activity in MN9D cells
    • Wu B, Liu Q, Duan C, et al. Phosphorylation of α-synuclein upregulates tyrosine hydroxylase activity in MN9D cells. Acta Histochem 2011;113:32-35.
    • (2011) Acta Histochem , vol.113 , pp. 32-35
    • Wu, B.1    Liu, Q.2    Duan, C.3
  • 119
    • 0036278335 scopus 로고    scopus 로고
    • Dopamine-dependent neurotoxicity of a-synuclein: a mechanism for selective neurodegeneration in Parkinson disease
    • Xu J, Kao S-Y, Lee FJS, et al. Dopamine-dependent neurotoxicity of a-synuclein: a mechanism for selective neurodegeneration in Parkinson disease. Nat Med 2002;8:600-606.
    • (2002) Nat Med , vol.8 , pp. 600-606
    • Xu, J.1    Kao, S.-Y.2    Lee, F.J.S.3
  • 120
    • 0034714204 scopus 로고    scopus 로고
    • Synucleins are a novel class of substrates for G protein-coupled receptor kinases
    • Pronin AN, Morris AJ, Surguchov A, Benovic JL. Synucleins are a novel class of substrates for G protein-coupled receptor kinases. J Biol Chem 2000;275:26515-26522.
    • (2000) J Biol Chem , vol.275 , pp. 26515-26522
    • Pronin, A.N.1    Morris, A.J.2    Surguchov, A.3    Benovic, J.L.4
  • 121
    • 84857693190 scopus 로고    scopus 로고
    • Phosphorylation of α-synuclein protein at Ser-129 reduces neuronal dysfunction by lowering its membrane binding property in Caenorhabditis elegans
    • Kuwahara T, Tonegawa R, Ito G, et al. Phosphorylation of α-synuclein protein at Ser-129 reduces neuronal dysfunction by lowering its membrane binding property in Caenorhabditis elegans. J Biol Chem 2012;287:7098-7109.
    • (2012) J Biol Chem , vol.287 , pp. 7098-7109
    • Kuwahara, T.1    Tonegawa, R.2    Ito, G.3
  • 122
    • 78649425814 scopus 로고    scopus 로고
    • PML regulates apoptosis at endoplasmic reticulum by modulating calcium release
    • Giorgi C, Ito K, Lin H-K, et al. PML regulates apoptosis at endoplasmic reticulum by modulating calcium release. Science 2010;330:1247-1251.
    • (2010) Science , vol.330 , pp. 1247-1251
    • Giorgi, C.1    Ito, K.2    Lin, H.-K.3
  • 123
    • 33749162349 scopus 로고    scopus 로고
    • Isoform- and subcellular fraction-specific differences in hippocampal 14-3-3 levels following experimentally evoked seizures and in human temporal lobe epilepsy
    • Schindler CK, Heverin M, Henshall DC. Isoform- and subcellular fraction-specific differences in hippocampal 14-3-3 levels following experimentally evoked seizures and in human temporal lobe epilepsy. J Neurochem 2006;99:561-569.
    • (2006) J Neurochem , vol.99 , pp. 561-569
    • Schindler, C.K.1    Heverin, M.2    Henshall, D.C.3
  • 124
    • 0025840551 scopus 로고
    • Ultrastructural localization of tyrosine hydroxylase immunoreactivity in the rat diagonal band of Broca
    • Milner TA. Ultrastructural localization of tyrosine hydroxylase immunoreactivity in the rat diagonal band of Broca. J Neurosci Res 1991;30:498-511.
    • (1991) J Neurosci Res , vol.30 , pp. 498-511
    • Milner, T.A.1
  • 125
    • 0016638416 scopus 로고
    • Ultrastructural localization of tyrosine hydroxylase in noradrenergic neurons of brain
    • Pickel VM, Joh TH, Reis DJ. Ultrastructural localization of tyrosine hydroxylase in noradrenergic neurons of brain. Proc Natl Acad Sci U S A 1975;72:659-663.
    • (1975) Proc Natl Acad Sci U S A , vol.72 , pp. 659-663
    • Pickel, V.M.1    Joh, T.H.2    Reis, D.J.3
  • 126
    • 84876083282 scopus 로고    scopus 로고
    • Role of Ser129 phosphorylation of α-synuclein in melanoma cells
    • Lee BR, Matsuo Y, Cashikar AG, Kamitani T. Role of Ser129 phosphorylation of α-synuclein in melanoma cells. J Cell Sci 2013;126:696-704.
    • (2013) J Cell Sci , vol.126 , pp. 696-704
    • Lee, B.R.1    Matsuo, Y.2    Cashikar, A.G.3    Kamitani, T.4
  • 128
    • 0000443658 scopus 로고
    • Diffuse intracytoplasmic ganglionic inclusions (Lewy type) associated with progressive dementia and quadriparesis in flexion
    • Okazaki H, Lipkin LE, Aronson SM. Diffuse intracytoplasmic ganglionic inclusions (Lewy type) associated with progressive dementia and quadriparesis in flexion. J Neuropathol Exp Neurol 1961;20:237-244.
    • (1961) J Neuropathol Exp Neurol , vol.20 , pp. 237-244
    • Okazaki, H.1    Lipkin, L.E.2    Aronson, S.M.3
  • 129
    • 78650356896 scopus 로고    scopus 로고
    • Phosphorylated a-synuclein at Ser-129 is targeted to the proteasome pathway in a ubiquitin-independent manner
    • Machiya Y, Hara S, Arawaka S, et al. Phosphorylated a-synuclein at Ser-129 is targeted to the proteasome pathway in a ubiquitin-independent manner. J Biol Chem 2010;285:40732-40744.
    • (2010) J Biol Chem , vol.285 , pp. 40732-40744
    • Machiya, Y.1    Hara, S.2    Arawaka, S.3
  • 130
    • 3042655068 scopus 로고    scopus 로고
    • Could a loss of a-synuclein function put dopaminergic neurons at risk?
    • Perez RG, Hastings TG. Could a loss of a-synuclein function put dopaminergic neurons at risk? J Neurochem 2004;89:1318-1324.
    • (2004) J Neurochem , vol.89 , pp. 1318-1324
    • Perez, R.G.1    Hastings, T.G.2


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