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Volumn 6, Issue 1, 2016, Pages 39-51

Implication of Alpha-Synuclein Phosphorylation at S129 in Synucleinopathies: What Have We Learned in the Last Decade?

Author keywords

animal models; biomarker; cell based assays; degradation; kinases; membrane binding; Phosphorylation; subcellular localization; toxicity

Indexed keywords

ALPHA SYNUCLEIN; METAL ION; SERINE;

EID: 84963780977     PISSN: 18777171     EISSN: 1877718X     Source Type: Journal    
DOI: 10.3233/JPD-160779     Document Type: Review
Times cited : (245)

References (129)
  • 2
    • 0032531924 scopus 로고    scopus 로고
    • Parkinson's disease. Second of two parts
    • Lang AE, & Lozano AM (1998) Parkinson's disease. Second of two parts. N Engl J Med, 339, 1130-1143.
    • (1998) N Engl J Med , vol.339 , pp. 1130-1143
    • Lang, A.E.1    Lozano, A.M.2
  • 4
    • 0032584686 scopus 로고    scopus 로고
    • Filamentous alpha-synuclein inclusions link multiple system atrophy with Parkinson's disease and dementia with Lewy bodies
    • Spillantini MG, Crowther RA, Jakes R, Cairns NJ, Lantos PL, & Goedert M (1998) Filamentous alpha-synuclein inclusions link multiple system atrophy with Parkinson's disease and dementia with Lewy bodies. Neurosci Lett, 251, 205-208.
    • (1998) Neurosci Lett , vol.251 , pp. 205-208
    • Spillantini, M.G.1    Crowther, R.A.2    Jakes, R.3    Cairns, N.J.4    Lantos, P.L.5    Goedert, M.6
  • 5
    • 0032568534 scopus 로고    scopus 로고
    • Alpha-Synuclein in filamentous inclusions of Lewy bodies from Parkinson's disease and dementia with Lewy bodies
    • Spillantini MG, Crowther RA, Jakes R, Hasegawa M, & Goedert M (1998) alpha-Synuclein in filamentous inclusions of Lewy bodies from Parkinson's disease and dementia with Lewy bodies. Proc Natl Acad Sci U S A, 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
  • 6
    • 84871414210 scopus 로고    scopus 로고
    • The many faces of alpha-synuclein: From structure and toxicity to therapeutic target
    • Lashuel HA, Overk CR, Oueslati A, & Masliah E (2013) The many faces of alpha-synuclein: From structure and toxicity to therapeutic target. Nat Rev Neurosci, 14, 38-48.
    • (2013) Nat Rev Neurosci , vol.14 , pp. 38-48
    • Lashuel, H.A.1    Overk, C.R.2    Oueslati, A.3    Masliah, E.4
  • 7
    • 33749240943 scopus 로고    scopus 로고
    • Mechanisms of Parkinson's disease linked to pathological alpha-synuclein: New targets for drug discovery
    • LeeVM,& Trojanowski JQ (2006) Mechanisms of Parkinson's disease linked to pathological alpha-synuclein: New targets for drug discovery. Neuron, 52, 33-38.
    • (2006) Neuron , vol.52 , pp. 33-38
    • Lee, V.M.1    Trojanowski, J.Q.2
  • 8
    • 77955366745 scopus 로고    scopus 로고
    • Role of post-translational modifications in modulating the structure, function and toxicity of alpha-synuclein: Implications for Parkinson's disease pathogenesis and therapies
    • Oueslati A, Fournier M, & Lashuel HA (2010) Role of post-translational modifications in modulating the structure, function and toxicity of alpha-synuclein: Implications for Parkinson's disease pathogenesis and therapies. Prog Brain Res, 183, 115-145.
    • (2010) Prog Brain Res , vol.183 , pp. 115-145
    • Oueslati, A.1    Fournier, M.2    Lashuel, H.A.3
  • 9
    • 84901364520 scopus 로고    scopus 로고
    • Protein phosphorylation in neurodegeneration: Friend or foe?
    • Tenreiro S, Eckermann K, & Outeiro TF (2014) Protein phosphorylation in neurodegeneration: Friend or foe? Front Mol Neurosci, 7, 42.
    • (2014) Front Mol Neurosci , vol.7 , pp. 42
    • Tenreiro, S.1    Eckermann, K.2    Outeiro, T.F.3
  • 10
    • 84855188545 scopus 로고    scopus 로고
    • Alpha-synuclein phosphorylation and truncation are normal events in the adult human brain
    • Muntane G, Ferrer I, & Martinez-Vicente M (2012) alpha-synuclein phosphorylation and truncation are normal events in the adult human brain. Neuroscience, 200, 106-119.
    • (2012) Neuroscience , vol.200 , pp. 106-119
    • Muntane, G.1    Ferrer, I.2    Martinez-Vicente, M.3
  • 13
    • 0034527763 scopus 로고    scopus 로고
    • Physiology and pathophysiology of alpha-synuclein. Cell culture and transgenic animal models based on a Parkinson's disease-associated protein
    • Kahle PJ, Neumann M, Ozmen L, & Haass C (2000) Physiology and pathophysiology of alpha-synuclein. Cell culture and transgenic animal models based on a Parkinson's disease-associated protein. Ann N Y Acad Sci, 920, 33-41.
    • (2000) Ann N y Acad Sci , vol.920 , pp. 33-41
    • Kahle, P.J.1    Neumann, M.2    Ozmen, L.3    Haass, C.4
  • 16
    • 0037461582 scopus 로고    scopus 로고
    • Phosphorylation of alpha-synuclein characteristic of synucleinopathy lesions is recapitulated in alpha-synuclein transgenic Drosophila
    • Takahashi M, Kanuka H, Fujiwara H, Koyama A, Hasegawa M, Miura M, & Iwatsubo T (2003) Phosphorylation of alpha-synuclein characteristic of synucleinopathy lesions is recapitulated in alpha-synuclein transgenic Drosophila. Neurosci Lett, 336, 155-158.
    • (2003) Neurosci Lett , vol.336 , pp. 155-158
    • Takahashi, M.1    Kanuka, H.2    Fujiwara, H.3    Koyama, A.4    Hasegawa, M.5    Miura, M.6    Iwatsubo, T.7
  • 17
    • 5444249974 scopus 로고    scopus 로고
    • Overexpression of alpha-synuclein in rat substantia nigra results in loss of dopaminergic neurons, phosphorylation of alpha-synuclein and activation of caspase-9: Resemblance to pathogenetic changes in Parkinson's disease
    • Yamada M, Iwatsubo T, MizunoY,& MochizukiH(2004) Overexpression of alpha-synuclein in rat substantia nigra results in loss of dopaminergic neurons, phosphorylation of alpha-synuclein and activation of caspase-9: Resemblance to pathogenetic changes in Parkinson's disease. J Neurochem, 91, 451-461.
    • (2004) J Neurochem , vol.91 , pp. 451-461
    • Yamada, M.1    Iwatsubo, T.2    Mizuno, Y.3    Mochizuki, H.4
  • 18
    • 17844406856 scopus 로고    scopus 로고
    • Alpha-synuclein phosphorylation controls neurotoxicity and inclusion formation in a Drosophila model of Parkinson disease
    • Chen L, & Feany MB (2005) Alpha-synuclein phosphorylation controls neurotoxicity and inclusion formation in a Drosophila model of Parkinson disease. Nat Neurosci, 8, 657-663.
    • (2005) Nat Neurosci , vol.8 , pp. 657-663
    • Chen, L.1    Feany, M.B.2
  • 20
    • 80052398365 scopus 로고    scopus 로고
    • Alpha-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation
    • Bartels T, Choi JG, & Selkoe DJ (2011) alpha-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation. Nature, 477, 107-110.
    • (2011) Nature , vol.477 , pp. 107-110
    • Bartels, T.1    Choi, J.G.2    Selkoe, D.J.3
  • 21
    • 84865249504 scopus 로고    scopus 로고
    • Characterization of semisynthetic and naturally Nalpha-acetylated alpha-synuclein in vitro and in intact cells: Implications for aggregation and cellular properties of alpha-synuclein
    • Fauvet B, Fares MB, Samuel F, Dikiy I, Tandon A, Eliezer D, & Lashuel HA (2012) Characterization of semisynthetic and naturally Nalpha-acetylated alpha-synuclein in vitro and in intact cells: Implications for aggregation and cellular properties of alpha-synuclein. J Biol Chem, 287, 28243-28262.
    • (2012) J Biol Chem , vol.287 , pp. 28243-28262
    • Fauvet, B.1    Fares, M.B.2    Samuel, F.3    Dikiy, I.4    Tandon, A.5    Eliezer, D.6    Lashuel, H.A.7
  • 22
    • 12944304172 scopus 로고    scopus 로고
    • Mapping long-range interactions in alpha-synuclein using spin-label NMR and ensemble molecular dynamics simulations
    • Dedmon MM, Lindorff-Larsen K, Christodoulou J, Vendruscolo M, & Dobson CM (2005) Mapping long-range interactions in alpha-synuclein using spin-label NMR and ensemble molecular dynamics simulations. J Am Chem Soc, 127, 476-477.
    • (2005) J Am Chem Soc , vol.127 , pp. 476-477
    • Dedmon, M.M.1    Lindorff-Larsen, K.2    Christodoulou, J.3    Vendruscolo, M.4    Dobson, C.M.5
  • 23
    • 42649142233 scopus 로고    scopus 로고
    • Characterization of conformational and dynamic properties of natively unfolded human and mouse alpha-synuclein ensembles by NMR: Implication for aggregation
    • Wu KP, Kim S, Fela DA, & Baum J (2008) Characterization of conformational and dynamic properties of natively unfolded human and mouse alpha-synuclein ensembles by NMR: Implication for aggregation. J Mol Biol, 378, 1104-1115.
    • (2008) J Mol Biol , vol.378 , pp. 1104-1115
    • Wu, K.P.1    Kim, S.2    Fela, D.A.3    Baum, J.4
  • 25
    • 84883079994 scopus 로고    scopus 로고
    • In-cell NMR characterization of the secondary structure populations of a disordered conformation of alphasynuclein within E. Coli cells
    • Waudby CA, Camilloni C, Fitzpatrick AW, Cabrita LD, Dobson CM, Vendruscolo M, & Christodoulou J (2013) In-cell NMR characterization of the secondary structure populations of a disordered conformation of alphasynuclein within E. coli cells. PLoS One, 8, e72286.
    • (2013) PLoS One , vol.8 , pp. e72286
    • Waudby, C.A.1    Camilloni, C.2    Fitzpatrick, A.W.3    Cabrita, L.D.4    Dobson, C.M.5    Vendruscolo, M.6    Christodoulou, J.7
  • 26
    • 35548988910 scopus 로고    scopus 로고
    • Paramagnetism-based NMR restraints provide maximum allowed probabilities for the different conformations of partially independent protein domains
    • Bertini I, Gupta YK, Luchinat C, Parigi G, Peana M, Sgheri L, & Yuan J (2007) Paramagnetism-based NMR restraints provide maximum allowed probabilities for the different conformations of partially independent protein domains. J Am Chem Soc, 129, 12786-12794.
    • (2007) J Am Chem Soc , vol.129 , pp. 12786-12794
    • Bertini, I.1    Gupta, Y.K.2    Luchinat, C.3    Parigi, G.4    Peana, M.5    Sgheri, L.6    Yuan, J.7
  • 27
    • 0035815115 scopus 로고    scopus 로고
    • Conformational properties of alpha-synuclein in its free and lipid-associated states
    • Eliezer D, Kutluay E, Bussell R Jr, & Browne G (2001) Conformational properties of alpha-synuclein in its free and lipid-associated states. J Mol Biol, 307, 1061-1073.
    • (2001) J Mol Biol , vol.307 , pp. 1061-1073
    • Eliezer, D.1    Kutluay, E.2    Bussell, R.3    Browne, G.4
  • 28
    • 27344436619 scopus 로고    scopus 로고
    • Structure and properties of alphasynuclein and other amyloids determined at the amino acid level
    • Del Mar C, Greenbaum EA, Mayne L, Englander SW, & Woods VL Jr (2005) Structure and properties of alphasynuclein and other amyloids determined at the amino acid level. Proc Natl Acad Sci U S A, 102, 15477-15482.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 15477-15482
    • Del Mar, C.1    Greenbaum, E.A.2    Mayne, L.3    Englander, S.W.4    Woods, V.L.5
  • 29
    • 8544264563 scopus 로고    scopus 로고
    • Double-stranded DNA stimulates the fibrillation of alphasynuclein in vitro and is associated with the mature fibrils: An electron microscopy study
    • Cherny D, HoyerW, Subramaniam V, & Jovin TM (2004) Double-stranded DNA stimulates the fibrillation of alphasynuclein in vitro and is associated with the mature fibrils: An electron microscopy study. J Mol Biol, 344, 929-938.
    • (2004) J Mol Biol , vol.344 , pp. 929-938
    • Cherny, D.1    Hoyer, W.2    Subramaniam, V.3    Jovin, T.M.4
  • 32
    • 0033520474 scopus 로고    scopus 로고
    • Alpha-synuclein binds to Tau and stimulates the protein kinase A-catalyzed tau phosphorylation of serine residues 262 and 356
    • Jensen PH, Hager H, Nielsen MS, Hojrup P, Gliemann J, & Jakes R (1999) alpha-synuclein binds to Tau and stimulates the protein kinase A-catalyzed tau phosphorylation of serine residues 262 and 356. J Biol Chem, 274, 25481-25489.
    • (1999) J Biol Chem , vol.274 , pp. 25481-25489
    • Jensen, P.H.1    Hager, H.2    Nielsen, M.S.3    Hojrup, P.4    Gliemann, J.5    Jakes, R.6
  • 33
    • 0034647557 scopus 로고    scopus 로고
    • Microtubule-associated protein 1B is a component of cortical Lewy bodies and binds alpha-synuclein filaments
    • Jensen PH, Islam K,Kenney J, Nielsen MS, Power J,& Gai WP (2000) Microtubule-associated protein 1B is a component of cortical Lewy bodies and binds alpha-synuclein filaments. J Biol Chem, 275, 21500-21507.
    • (2000) J Biol Chem , vol.275 , pp. 21500-21507
    • Jensen, P.H.1    Islam, K.2    Kenney, J.3    Nielsen, M.S.4    Power, J.5    Gai, W.P.6
  • 34
    • 79959925894 scopus 로고    scopus 로고
    • Alphasynuclein interacts with Glucocerebrosidase providing a molecular link between Parkinson and Gaucher diseases
    • Yap TL, Gruschus JM, Velayati A, Westbroek W, Goldin E, Moaven N, Sidransky E, & Lee JC (2011) Alphasynuclein interacts with Glucocerebrosidase providing a molecular link between Parkinson and Gaucher diseases. J Biol Chem, 286, 28080-28088.
    • (2011) J Biol Chem , vol.286 , pp. 28080-28088
    • Yap, T.L.1    Gruschus, J.M.2    Velayati, A.3    Westbroek, W.4    Goldin, E.5    Moaven, N.6    Sidransky, E.7    Lee, J.C.8
  • 35
    • 34447629079 scopus 로고    scopus 로고
    • Interactions between metals and alphasynuclein-function or artefact?
    • Brown DR (2007) Interactions between metals and alphasynuclein-function or artefact? FEBS J, 274, 3766-3774.
    • (2007) FEBS J , vol.274 , pp. 3766-3774
    • Brown, D.R.1
  • 36
    • 0033564726 scopus 로고    scopus 로고
    • Copper(II)-induced self-oligomerization of alphasynuclein
    • Paik SR, Shin HJ, Lee JH, Chang CS, & Kim J (1999) Copper(II)-induced self-oligomerization of alphasynuclein. Biochem J, 340(Pt 3), 821-828.
    • (1999) Biochem J , vol.340 , pp. 821-828
    • Paik, S.R.1    Shin, H.J.2    Lee, J.H.3    Chang, C.S.4    Kim, J.5
  • 37
    • 8544264002 scopus 로고    scopus 로고
    • Impact of the acidic C-terminal region comprising amino acids 109-140 on alpha-synuclein aggregation in vitro
    • HoyerW, Cherny D, Subramaniam V, & Jovin TM (2004) Impact of the acidic C-terminal region comprising amino acids 109-140 on alpha-synuclein aggregation in vitro. Biochemistry, 43, 16233-16242.
    • (2004) Biochemistry , vol.43 , pp. 16233-16242
    • Hoyer, W.1    Cherny, D.2    Subramaniam, V.3    Jovin, T.M.4
  • 38
    • 67349196431 scopus 로고    scopus 로고
    • Dissecting the mechanisms of tissue transglutaminase-induced cross-linking of alpha-synuclein: Implications for the pathogenesis of Parkinson disease
    • Schmid AW, Chiappe D, Pignat V, Grimminger V, Hang I, Moniatte M, & Lashuel HA (2009) Dissecting the mechanisms of tissue transglutaminase-induced cross-linking of alpha-synuclein: Implications for the pathogenesis of Parkinson disease. J Biol Chem, 284, 13128-13142.
    • (2009) J Biol Chem , vol.284 , pp. 13128-13142
    • Schmid, A.W.1    Chiappe, D.2    Pignat, V.3    Grimminger, V.4    Hang, I.5    Moniatte, M.6    Lashuel, H.A.7
  • 39
    • 84937730909 scopus 로고    scopus 로고
    • Alpha-synuclein function and dysfunction on cellular membranes
    • Snead D, & Eliezer D (2014) Alpha-synuclein function and dysfunction on cellular membranes. Exp Neurobiol, 23, 292-313.
    • (2014) Exp Neurobiol , vol.23 , pp. 292-313
    • Snead, D.1    Eliezer, D.2
  • 40
    • 84857649648 scopus 로고    scopus 로고
    • Folding and misfolding of alpha-synuclein on membranes
    • Dikiy I, & Eliezer D (2012) Folding and misfolding of alpha-synuclein on membranes. Biochim Biophys Acta, 1818, 1013-1018.
    • (2012) Biochim Biophys Acta , vol.1818 , pp. 1013-1018
    • Dikiy, I.1    Eliezer, D.2
  • 41
    • 84855444970 scopus 로고    scopus 로고
    • Biophysics of alpha-synuclein membrane interactions
    • Pfefferkorn CM, Jiang Z, & Lee JC (2012) Biophysics of alpha-synuclein membrane interactions. Biochim Biophys Acta, 1818, 162-171.
    • (2012) Biochim Biophys Acta , vol.1818 , pp. 162-171
    • Pfefferkorn, C.M.1    Jiang, Z.2    Lee, J.C.3
  • 44
    • 0034714204 scopus 로고    scopus 로고
    • Synucleins are a novel class of substrates for G proteincoupled receptor kinases
    • Pronin AN, Morris AJ, SurguchovA,& Benovic JL (2000) Synucleins are a novel class of substrates for G proteincoupled receptor kinases. J Biol Chem, 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
  • 45
    • 84902578862 scopus 로고    scopus 로고
    • Modelling Ser129 phosphorylation inhibits membrane binding of pore-forming alpha-synuclein oligomers
    • Nubling GS, Levin J, Bader B, Lorenzl S, Hillmer A, Hogen T, Kamp F, & Giese A (2014) Modelling Ser129 phosphorylation inhibits membrane binding of pore-forming alpha-synuclein oligomers. PLoS One, 9, e98906.
    • (2014) PLoS One , vol.9 , pp. e98906
    • Nubling, G.S.1    Levin, J.2    Bader, B.3    Lorenzl, S.4    Hillmer, A.5    Hogen, T.6    Kamp, F.7    Giese, A.8
  • 47
    • 84857693190 scopus 로고    scopus 로고
    • Phosphorylation of alpha-synuclein protein at Ser-129 reduces neuronal dysfunction by lowering its membrane binding property in Caenorhabditis elegans
    • Kuwahara T, Tonegawa R, Ito G, Mitani S, & Iwatsubo T (2012) Phosphorylation of alpha-synuclein protein at Ser-129 reduces neuronal dysfunction by lowering its membrane binding property in Caenorhabditis elegans. J Biol Chem, 287, 7098-7109.
    • (2012) J Biol Chem , vol.287 , pp. 7098-7109
    • Kuwahara, T.1    Tonegawa, R.2    Ito, G.3    Mitani, S.4    Iwatsubo, T.5
  • 49
    • 84878682977 scopus 로고    scopus 로고
    • Serine 129 phosphorylation of membrane-associated alpha-synuclein modulates dopamine transporter function in a G protein-coupled receptor kinase-dependent manner
    • S1641-1643
    • Hara S, Arawaka S, Sato H, Machiya Y, Cui C, Sasaki A, Koyama S, & Kato T (2013) Serine 129 phosphorylation of membrane-associated alpha-synuclein modulates dopamine transporter function in a G protein-coupled receptor kinase-dependent manner. Mol Biol Cell 24, 1649-1660, S1641-1643.
    • (2013) Mol Biol Cell , vol.24 , pp. 1649-1660
    • Hara, S.1    Arawaka, S.2    Sato, H.3    Machiya, Y.4    Cui, C.5    Sasaki, A.6    Koyama, S.7    Kato, T.8
  • 50
    • 4143067071 scopus 로고    scopus 로고
    • Phosphorylated alpha-synuclein in normal mouse brain
    • Hirai Y, Fujita SC, Iwatsubo T, & Hasegawa M (2004) Phosphorylated alpha-synuclein in normal mouse brain. FEBS Lett, 572, 227-232.
    • (2004) FEBS Lett , vol.572 , pp. 227-232
    • Hirai, Y.1    Fujita, S.C.2    Iwatsubo, T.3    Hasegawa, M.4
  • 51
    • 72949084639 scopus 로고    scopus 로고
    • Interaction between alpha-synuclein and metal ions, still looking for a role in the pathogenesis of Parkinson's disease
    • Bisaglia M, Tessari I, Mammi S, & Bubacco L (2009) Interaction between alpha-synuclein and metal ions, still looking for a role in the pathogenesis of Parkinson's disease. Neuromolecular Med, 11, 239-251.
    • (2009) Neuromolecular Med , vol.11 , pp. 239-251
    • Bisaglia, M.1    Tessari, I.2    Mammi, S.3    Bubacco, L.4
  • 52
    • 33846671209 scopus 로고    scopus 로고
    • Phosphorylation-dependent metal binding by alpha-synuclein peptide fragments
    • Liu LL, & Franz KJ (2007) Phosphorylation-dependent metal binding by alpha-synuclein peptide fragments. J Biol Inorg Chem, 12, 234-247.
    • (2007) J Biol Inorg Chem , vol.12 , pp. 234-247
    • Liu, L.L.1    Franz, K.J.2
  • 53
    • 81455136019 scopus 로고    scopus 로고
    • Phosphorylation of alpha-Synuclein at Y125 and S129 alters its metal binding properties: Implications for understanding the role of alpha-Synuclein in the pathogenesis of Parkinson's Disease and related disorders
    • Lu Y, Prudent M, Fauvet B, Lashuel HA, & Girault HH (2011) Phosphorylation of alpha-Synuclein at Y125 and S129 alters its metal binding properties: Implications for understanding the role of alpha-Synuclein in the pathogenesis of Parkinson's Disease and related disorders. ACS Chem Neurosci, 2, 667-675.
    • (2011) ACS Chem Neurosci , vol.2 , pp. 667-675
    • Lu, Y.1    Prudent, M.2    Fauvet, B.3    Lashuel, H.A.4    Girault, H.H.5
  • 54
    • 33746633380 scopus 로고    scopus 로고
    • Interaction of alpha-synuclein with divalent metal ions reveals key differences: A link between structure, binding specificity and fibrillation enhancement
    • Binolfi A, Rasia RM, Bertoncini CW, Ceolin M, ZweckstetterM, Griesinger C, JovinTM,& FernandezCO(2006) Interaction of alpha-synuclein with divalent metal ions reveals key differences: A link between structure, binding specificity and fibrillation enhancement. J Am Chem Soc, 128, 9893-9901.
    • (2006) J Am Chem Soc , vol.128 , pp. 9893-9901
    • Binolfi, A.1    Rasia, R.M.2    Bertoncini, C.W.3    Ceolin, M.4    Zweckstetter, M.5    Griesinger, C.6    Jovin, T.M.7    Fernandez, C.O.8
  • 60
  • 61
    • 84891300736 scopus 로고    scopus 로고
    • Ubiquitination increases parkin activity to promote autophagic alpha-synuclein clearance
    • Lonskaya I, Desforges NM, Hebron ML, & Moussa CE (2013) Ubiquitination increases parkin activity to promote autophagic alpha-synuclein clearance. PLoS One, 8, e83914.
    • (2013) PLoS One , vol.8 , pp. e83914
    • Lonskaya, I.1    Desforges, N.M.2    Hebron, M.L.3    Moussa, C.E.4
  • 62
    • 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 (2014) Interplay between sumoylation and phosphorylation for protection against alpha-synuclein inclusions. J Biol Chem, 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
  • 64
    • 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 (2013) Nilotinib reverses loss of dopamine neurons and improves motor behavior via autophagic degradation of alpha-synuclein in Parkinson's disease models. Hum Mol Genet, 22, 3315-3328.
    • (2013) Hum Mol Genet , vol.22 , pp. 3315-3328
    • Hebron, M.L.1    Lonskaya, I.2    Moussa, C.E.3
  • 65
    • 67650496503 scopus 로고    scopus 로고
    • Relationship between alpha synuclein phosphorylation, proteasomal inhibition and cell death: Relevance to Parkinson's disease pathogenesis
    • Chau KY, Ching HL, Schapira AH, & Cooper JM (2009) Relationship between alpha synuclein phosphorylation, proteasomal inhibition and cell death: Relevance to Parkinson's disease pathogenesis. J Neurochem, 110, 1005-1013.
    • (2009) J Neurochem , vol.110 , pp. 1005-1013
    • Chau, K.Y.1    Ching, H.L.2    Schapira, A.H.3    Cooper, J.M.4
  • 66
    • 78650356896 scopus 로고    scopus 로고
    • Phosphorylated alpha-synuclein at Ser-129 is targeted to the proteasome pathway in a ubiquitin-independent manner
    • Machiya Y, Hara S, Arawaka S, Fukushima S, Sato H, Sakamoto M,Koyama S,& Kato T (2010) Phosphorylated alpha-synuclein at Ser-129 is targeted to the proteasome pathway in a ubiquitin-independent manner. J Biol Chem, 285, 40732-40744.
    • (2010) J Biol Chem , vol.285 , pp. 40732-40744
    • Machiya, Y.1    Hara, S.2    Arawaka, S.3    Fukushima, S.4    Sato, H.5    Sakamoto, M.6    Koyama, S.7    Kato, T.8
  • 70
    • 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 (2013) Polo-like kinase 2 regulates selective autophagic alpha-synuclein clearance and suppresses its toxicity in vivo. Proc Natl Acad Sci U S A, 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
  • 72
    • 13244249573 scopus 로고    scopus 로고
    • Polo-like kinases in the nervous system
    • Seeburg DP, Pak D, & Sheng M (2005) Polo-like kinases in the nervous system. Oncogene, 24, 292-298.
    • (2005) Oncogene , vol.24 , pp. 292-298
    • Seeburg, D.P.1    Pak, D.2    Sheng, M.3
  • 73
    • 43649097642 scopus 로고    scopus 로고
    • Critical role of CDK5 and Polo-like kinase 2 in homeostatic synaptic plasticity during elevated activity
    • SeeburgDP, Feliu-Mojer M, Gaiottino J, PakDT,& Sheng M (2008) Critical role of CDK5 and Polo-like kinase 2 in homeostatic synaptic plasticity during elevated activity. Neuron, 58, 571-583.
    • (2008) Neuron , vol.58 , pp. 571-583
    • Seeburg, D.P.1    Feliu-Mojer, M.2    Gaiottino, J.3    Pak, D.T.4    Sheng, M.5
  • 74
    • 84952645933 scopus 로고    scopus 로고
    • The Synaptic Function of alpha-Synuclein
    • Burre J (2015) The Synaptic Function of alpha-Synuclein. J Parkinsons Dis, 5(4), 699-713.
    • (2015) J Parkinsons Dis , vol.5 , Issue.4 , pp. 699-713
    • Burre, J.1
  • 76
    • 84903152487 scopus 로고    scopus 로고
    • Polo-like kinase 2 activates an antioxidant pathway to promote the survival of cells with mitochondrial dysfunction
    • Li J, Ma W, Wang PY, Hurley PJ, Bunz F, & Hwang PM (2014) Polo-like kinase 2 activates an antioxidant pathway to promote the survival of cells with mitochondrial dysfunction. Free Radic Biol Med, 73, 270-277.
    • (2014) Free Radic Biol Med , vol.73 , pp. 270-277
    • Li, J.1    Ma, W.2    Wang, P.Y.3    Hurley, P.J.4    Bunz, F.5    Hwang, P.M.6
  • 77
    • 0037192865 scopus 로고    scopus 로고
    • Alpha-Synuclein protects against oxidative stress via inactivation of the c-Jun Nterminal kinase stress-signaling pathway in neuronal cells
    • Hashimoto M, Hsu LJ, Rockenstein E, Takenouchi T, Mallory M, & Masliah E (2002) alpha-Synuclein protects against oxidative stress via inactivation of the c-Jun Nterminal kinase stress-signaling pathway in neuronal cells. J Biol Chem, 277, 11465-11472.
    • (2002) J Biol Chem , vol.277 , pp. 11465-11472
    • Hashimoto, M.1    Hsu, L.J.2    Rockenstein, E.3    Takenouchi, T.4    Mallory, M.5    Masliah, E.6
  • 78
    • 57049151865 scopus 로고    scopus 로고
    • Proteomics analysis identifies phosphorylationdependent alpha-synuclein protein interactions
    • McFarland MA, Ellis CE, Markey SP, & Nussbaum RL (2008) Proteomics analysis identifies phosphorylationdependent alpha-synuclein protein interactions. Mol Cell Proteomics, 7, 2123-2137.
    • (2008) Mol Cell Proteomics , vol.7 , pp. 2123-2137
    • McFarland, M.A.1    Ellis, C.E.2    Markey, S.P.3    Nussbaum, R.L.4
  • 81
    • 84867787595 scopus 로고    scopus 로고
    • Systematic mutagenesis of alpha-synuclein reveals distinct sequence requirements for physiological and pathological activities
    • Burre J, Sharma M, & Sudhof TC (2012) Systematic mutagenesis of alpha-synuclein reveals distinct sequence requirements for physiological and pathological activities. J Neurosci, 32, 15227-15242.
    • (2012) J Neurosci , vol.32 , pp. 15227-15242
    • Burre, J.1    Sharma, M.2    Sudhof, T.C.3
  • 82
    • 0035500991 scopus 로고    scopus 로고
    • Protein-protein interactions of alpha-synuclein in brain homogenates and transfected cells
    • Payton JE, Perrin RJ, Clayton DF, & George JM (2001) Protein-protein interactions of alpha-synuclein in brain homogenates and transfected cells. Brain Res Mol Brain Res, 95, 138-145.
    • (2001) Brain Res Mol Brain Res , vol.95 , pp. 138-145
    • Payton, J.E.1    Perrin, R.J.2    Clayton, D.F.3    George, J.M.4
  • 83
    • 77956966416 scopus 로고    scopus 로고
    • Molecular interaction of alpha-synuclein with tubulin influences on the polymerization of microtubule in vitro and structure of microtubule in cells
    • Zhou RM, Huang YX, Li XL, Chen C, Shi Q, Wang GR, Tian C, Wang ZY, Jing YY, Gao C, & Dong XP (2010) Molecular interaction of alpha-synuclein with tubulin influences on the polymerization of microtubule in vitro and structure of microtubule in cells. Mol Biol Rep, 37, 3183-3192.
    • (2010) Mol Biol Rep , vol.37 , pp. 3183-3192
    • Zhou, R.M.1    Huang, Y.X.2    Li, X.L.3    Chen, C.4    Shi, Q.5    Wang, G.R.6    Tian, C.7    Wang, Z.Y.8    Jing, Y.Y.9    Gao, C.10    Dong, X.P.11
  • 84
    • 34848881102 scopus 로고    scopus 로고
    • Alpha-synuclein protects cerebellar granule neurons against 6-hydroxydopamine-induced death
    • Monti B, Polazzi E, Batti L, Crochemore C, Virgili M, & Contestabile A (2007) Alpha-synuclein protects cerebellar granule neurons against 6-hydroxydopamine-induced death. J Neurochem, 103, 518-530.
    • (2007) J Neurochem , vol.103 , pp. 518-530
    • Monti, B.1    Polazzi, E.2    Batti, L.3    Crochemore, C.4    Virgili, M.5    Contestabile, A.6
  • 85
    • 84887273441 scopus 로고    scopus 로고
    • Assessing the subcellular dynamics of alpha-synuclein using photoactivation microscopy
    • Goncalves S, & Outeiro TF (2013) Assessing the subcellular dynamics of alpha-synuclein using photoactivation microscopy. Mol Neurobiol, 47, 1081-1092.
    • (2013) Mol Neurobiol , vol.47 , pp. 1081-1092
    • Goncalves, S.1    Outeiro, T.F.2
  • 86
    • 84901188413 scopus 로고    scopus 로고
    • The nuclear accumulation of alphasynuclein is mediated by importin alpha and promotes neurotoxicity by accelerating the cell cycle
    • Ma KL, Song LK, Yuan YH, Zhang Y, Han N, Gao K, & Chen NH (2014) The nuclear accumulation of alphasynuclein is mediated by importin alpha and promotes neurotoxicity by accelerating the cell cycle. Neuropharmacology, 82, 132-142.
    • (2014) Neuropharmacology , vol.82 , pp. 132-142
    • Ma, K.L.1    Song, L.K.2    Yuan, Y.H.3    Zhang, Y.4    Han, N.5    Gao, K.6    Chen, N.H.7
  • 87
    • 84876083282 scopus 로고    scopus 로고
    • Role of Ser129 phosphorylation of alpha-synuclein in melanoma cells
    • Lee BR, Matsuo Y, Cashikar AG, & Kamitani T (2013) Role of Ser129 phosphorylation of alpha-synuclein in melanoma cells. J Cell Sci, 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
  • 88
    • 0033724436 scopus 로고    scopus 로고
    • Subcellular localization of alpha-synuclein in primary neuronal cultures: Effect of missense mutations
    • McLean PJ, Ribich S, & Hyman BT (2000) Subcellular localization of alpha-synuclein in primary neuronal cultures: Effect of missense mutations. J Neural Transm Suppl, 53-63.
    • (2000) J Neural Transm Suppl , pp. 53-63
    • McLean, P.J.1    Ribich, S.2    Hyman, B.T.3
  • 93
    • 64649106275 scopus 로고    scopus 로고
    • Nuclear and neuritic distribution of serine-129 phosphorylated alpha-synuclein in transgenic mice
    • Schell H, Hasegawa T, Neumann M, & Kahle PJ (2009) Nuclear and neuritic distribution of serine-129 phosphorylated alpha-synuclein in transgenic mice. Neuroscience, 160, 796-804.
    • (2009) Neuroscience , vol.160 , pp. 796-804
    • Schell, H.1    Hasegawa, T.2    Neumann, M.3    Kahle, P.J.4
  • 95
    • 33847649977 scopus 로고    scopus 로고
    • Extensive nuclear localization of alpha-synuclein in normal rat brain neurons revealed by a novel monoclonal antibody
    • Yu S, Li X, Liu G, Han J, Zhang C, Li Y, Xu S, Liu C, Gao Y, Yang H, Ueda K, & Chan P (2007) Extensive nuclear localization of alpha-synuclein in normal rat brain neurons revealed by a novel monoclonal antibody. Neuroscience, 145, 539-555.
    • (2007) Neuroscience , vol.145 , pp. 539-555
    • Yu, S.1    Li, X.2    Liu, G.3    Han, J.4    Zhang, C.5    Li, Y.6    Xu, S.7    Liu, C.8    Gao, Y.9    Yang, H.10    Ueda, K.11    Chan, P.12
  • 96
    • 83055176374 scopus 로고    scopus 로고
    • Determining nuclear localization of alpha-synuclein in mouse brains
    • Huang Z, Xu Z, Wu Y, & Zhou Y (2011) Determining nuclear localization of alpha-synuclein in mouse brains. Neuroscience, 199, 318-332.
    • (2011) Neuroscience , vol.199 , pp. 318-332
    • Huang, Z.1    Xu, Z.2    Wu, Y.3    Zhou, Y.4
  • 97
    • 84901338303 scopus 로고    scopus 로고
    • The novel Parkinson's disease linked mutation G51D attenuates in vitro aggregation and membrane binding of alpha-synuclein, and enhances its secretion and nuclear localization in cells
    • Fares MB, Ait-Bouziad N, Dikiy I, Mbefo MK, Jovicic A, Kiely A, Holton JL, Lee SJ, Gitler AD, Eliezer D, & Lashuel HA (2014) The novel Parkinson's disease linked mutation G51D attenuates in vitro aggregation and membrane binding of alpha-synuclein, and enhances its secretion and nuclear localization in cells.HumMol Genet, 23, 4491-4509.
    • (2014) HumMol Genet , vol.23 , pp. 4491-4509
    • Fares, M.B.1    Ait-Bouziad, N.2    Dikiy, I.3    Mbefo, M.K.4    Jovicic, A.5    Kiely, A.6    Holton, J.L.7    Lee, S.J.8    Gitler, A.D.9    Eliezer, D.10    Lashuel, H.A.11
  • 99
    • 84861534126 scopus 로고    scopus 로고
    • Increased alpha-synuclein phosphorylation and nitration in the aging primate substantia nigra
    • McCormack AL, Mak SK, & Di Monte DA (2012) Increased alpha-synuclein phosphorylation and nitration in the aging primate substantia nigra. Cell Death Dis, 3, e315.
    • (2012) Cell Death Dis , vol.3 , pp. e315
    • McCormack, A.L.1    Mak, S.K.2    Di Monte, D.A.3
  • 100
    • 84870820743 scopus 로고    scopus 로고
    • Age-dependent alpha-synuclein aggregation in the Microcebus murinus lemur primate
    • Canron MH, Perret M, Vital A, Bezard E, & Dehay B (2012) Age-dependent alpha-synuclein aggregation in the Microcebus murinus lemur primate. Sci Rep, 2, 910.
    • (2012) Sci Rep , vol.2 , pp. 910
    • Canron, M.H.1    Perret, M.2    Vital, A.3    Bezard, E.4    Dehay, B.5
  • 103
    • 84877352565 scopus 로고    scopus 로고
    • Ser129D mutant alpha-synuclein induces earlier motor dysfunction while S129A results in distinctive pathology in a rat model of Parkinson's disease
    • Febbraro F, Sahin G, Farran A, Soares S, Jensen PH, Kirik D, & Romero-Ramos M (2013) Ser129D mutant alpha-synuclein induces earlier motor dysfunction while S129A results in distinctive pathology in a rat model of Parkinson's disease. Neurobiol Dis, 56, 47-58.
    • (2013) Neurobiol Dis , vol.56 , pp. 47-58
    • Febbraro, F.1    Sahin, G.2    Farran, A.3    Soares, S.4    Jensen, P.H.5    Kirik, D.6    Romero-Ramos, M.7
  • 104
    • 67651008224 scopus 로고    scopus 로고
    • Lrrk2 phosphorylates alpha synuclein at serine 129: Parkinson disease implications
    • Qing H,WongW, McGeer EG,& McGeerPL(2009) Lrrk2 phosphorylates alpha synuclein at serine 129: Parkinson disease implications. Biochem Biophys Res Commun, 387, 149-152.
    • (2009) Biochem Biophys Res Commun , vol.387 , pp. 149-152
    • Qing, H.1    Wong, W.2    McGeer, E.G.3    McGeer, P.L.4
  • 105
    • 81255188869 scopus 로고    scopus 로고
    • Authentically phosphorylated alpha-synuclein at Ser129 accelerates neurodegeneration in a rat model of familial Parkinson's disease
    • Sato H, Arawaka S, Hara S, Fukushima S, Koga K, Koyama S,& Kato T (2011) Authentically phosphorylated alpha-synuclein at Ser129 accelerates neurodegeneration in a rat model of familial Parkinson's disease. J Neurosci, 31, 16884-16894.
    • (2011) J Neurosci , vol.31 , pp. 16884-16894
    • Sato, H.1    Arawaka, S.2    Hara, S.3    Fukushima, S.4    Koga, K.5    Koyama, S.6    Kato, T.7
  • 106
    • 84856507495 scopus 로고    scopus 로고
    • Superiority of PLK-2 as alpha-synuclein phosphorylating agent relies on unique specificity determinants
    • Salvi M, Trashi E, Marin O, Negro A, Sarno S,& PinnaLA (2012) Superiority of PLK-2 as alpha-synuclein phosphorylating agent relies on unique specificity determinants. Biochem Biophys Res Commun, 418, 156-160.
    • (2012) Biochem Biophys Res Commun , vol.418 , pp. 156-160
    • Salvi, M.1    Trashi, E.2    Marin, O.3    Negro, A.4    Sarno, S.5    Pinna, L.A.6
  • 109
    • 84924185649 scopus 로고    scopus 로고
    • Protein Transmission, Seeding and Degradation: Key Steps for alpha-Synuclein Prion-Like Propagation
    • Oueslati A, Ximerakis M, & Vekrellis K (2014) Protein Transmission, Seeding and Degradation: Key Steps for alpha-Synuclein Prion-Like Propagation. Exp Neurobiol, 23, 324-336.
    • (2014) Exp Neurobiol , vol.23 , pp. 324-336
    • Oueslati, A.1    Ximerakis, M.2    Vekrellis, K.3
  • 113
  • 116
    • 78650203006 scopus 로고    scopus 로고
    • Characterization of kinases involved in the phosphorylation of aggregated alpha-synuclein
    • Waxman EA, & Giasson BI (2011) Characterization of kinases involved in the phosphorylation of aggregated alpha-synuclein. J Neurosci Res, 89, 231-247.
    • (2011) J Neurosci Res , vol.89 , pp. 231-247
    • Waxman, E.A.1    Giasson, B.I.2
  • 117
    • 84856667162 scopus 로고    scopus 로고
    • Mimicking phosphorylation at serine 87 inhibits the aggregation of human alpha-synuclein and protects against its toxicity in a rat model of Parkinson's disease
    • Oueslati A, Paleologou KE, Schneider BL, Aebischer P,& Lashuel HA (2012) Mimicking phosphorylation at serine 87 inhibits the aggregation of human alpha-synuclein and protects against its toxicity in a rat model of Parkinson's disease. J Neurosci, 32, 1536-1544.
    • (2012) J Neurosci , vol.32 , pp. 1536-1544
    • Oueslati, A.1    Paleologou, K.E.2    Schneider, B.L.3    Aebischer, P.4    Lashuel, H.A.5
  • 122
  • 124
    • 84927922558 scopus 로고    scopus 로고
    • Evaluating the relationship between amyloid-beta and alpha-synuclein phosphorylated at Ser129 in dementia with Lewy bodies and Parkinson's disease
    • Swirski M, Miners JS, de Silva R, Lashley T, Ling H, Holton J, Revesz T, & Love S (2014) Evaluating the relationship between amyloid-beta and alpha-synuclein phosphorylated at Ser129 in dementia with Lewy bodies and Parkinson's disease. Alzheimers Res Ther, 6, 77.
    • (2014) Alzheimers Res Ther , vol.6 , pp. 77
    • Swirski, M.1    Miners, J.S.2    De Silva, R.3    Lashley, T.4    Ling, H.5    Holton, J.6    Revesz, T.7    Love, S.8
  • 125
    • 81955167983 scopus 로고    scopus 로고
    • Post mortem cerebrospinal fluid alpha-synuclein levels are raised in multiple system atrophy and distinguish this from the other alpha-synucleinopathies, Parkinson's disease and Dementia with Lewy bodies
    • Foulds PG, Yokota O, Thurston A, Davidson Y, Ahmed Z, Holton J, Thompson JC, Akiyama H, Arai T, Hasegawa M, Gerhard A, Allsop D, & Mann DM (2012) Post mortem cerebrospinal fluid alpha-synuclein levels are raised in multiple system atrophy and distinguish this from the other alpha-synucleinopathies, Parkinson's disease and Dementia with Lewy bodies. Neurobiol Dis, 45, 188-195.
    • (2012) Neurobiol Dis , vol.45 , pp. 188-195
    • Foulds, P.G.1    Yokota, O.2    Thurston, A.3    Davidson, Y.4    Ahmed, Z.5    Holton, J.6    Thompson, J.C.7    Akiyama, H.8    Arai, T.9    Hasegawa, M.10    Gerhard, A.11    Allsop, D.12    Mann, D.M.13
  • 127
    • 84918572460 scopus 로고    scopus 로고
    • Efficient modification of alpha-synuclein serine 129 by protein kinase CK1 requires phosphorylation of tyrosine 125 as a priming event
    • Kosten J, Binolfi A, Stuiver M, Verzini S, Theillet FX, Bekei B, van Rossum M, & Selenko P (2014) Efficient modification of alpha-synuclein serine 129 by protein kinase CK1 requires phosphorylation of tyrosine 125 as a priming event. ACS Chem Neurosci, 5, 1203-1208.
    • (2014) ACS Chem Neurosci , vol.5 , pp. 1203-1208
    • Kosten, J.1    Binolfi, A.2    Stuiver, M.3    Verzini, S.4    Theillet, F.X.5    Bekei, B.6    Van Rossum, M.7    Selenko, P.8
  • 128
    • 70449347241 scopus 로고    scopus 로고
    • Tyrosine and serine phosphorylation of alpha-synuclein have opposing effects on neurotoxicity and soluble oligomer formation
    • Chen L, Periquet M, Wang X, Negro A, McLean PJ, Hyman BT, & Feany MB (2009) Tyrosine and serine phosphorylation of alpha-synuclein have opposing effects on neurotoxicity and soluble oligomer formation. J Clin Invest, 119, 3257-3265.
    • (2009) J Clin Invest , vol.119 , pp. 3257-3265
    • Chen, L.1    Periquet, M.2    Wang, X.3    Negro, A.4    McLean, P.J.5    Hyman, B.T.6    Feany, M.B.7
  • 129
    • 15744362063 scopus 로고    scopus 로고
    • Structure and dynamics of micelle-bound human alphasynuclein
    • Ulmer TS, Bax A, Cole NB, & Nussbaum RL (2005) Structure and dynamics of micelle-bound human alphasynuclein. J Biol Chem, 280, 9595-9603.
    • (2005) J Biol Chem , vol.280 , pp. 9595-9603
    • Ulmer, T.S.1    Bax, A.2    Cole, N.B.3    Nussbaum, R.L.4


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