메뉴 건너뛰기




Volumn 5, Issue 12, 2014, Pages 1203-1208

Efficient modification of alpha-synuclein serine 129 by protein kinase CK1 requires phosphorylation of tyrosine 125 as a priming event

Author keywords

Alpha synuclein; Casein kinase 1; Kinetics; NMR; Parkinson's disease; Phosphorylation

Indexed keywords

ALPHA SYNUCLEIN; CASEIN KINASE I; FOCAL ADHESION KINASE 1; PROTEIN KINASE FYN; PROTEIN KINASE LYN; PROTEIN KINASE YES; PROTEIN TYROSINE KINASE; SERINE; GREEN FLUORESCENT PROTEIN; TYROSINE;

EID: 84918572460     PISSN: None     EISSN: 19487193     Source Type: Journal    
DOI: 10.1021/cn5002254     Document Type: Article
Times cited : (56)

References (38)
  • 1
    • 84871414210 scopus 로고    scopus 로고
    • The many faces of alpha-synuclein: From structure and toxicity to therapeutic target
    • Lashuel, H. A., Overk, C. R., Oueslati, A., and 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
  • 3
    • 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., and Lashuel, H. A. (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
  • 4
    • 84871414210 scopus 로고    scopus 로고
    • Lashuel, H. A., Overk, C. R., Oueslati, A., and Masliah, E. (2013) The many faces of alpha-synuclein: From structure and toxicity to therapeutic target. Nat. Rev. Neurosci. 14, 38-48.
    • (2013) , vol.14 , pp. 38-48
    • Lashuel, H.A.1    Overk, C.R.2    Oueslati, A.3    Masliah, E.4
  • 6
    • 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., and Lashuel, H. A. (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
  • 7
    • 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
    • Hara, S., Arawaka, S., Sato, H., Machiya, Y., Cui, C., Sasaki, A., Koyama, S., and 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 , Issue.1649-1660 , pp. S1641-S1643
    • Hara, S.1    Arawaka, S.2    Sato, H.3    Machiya, Y.4    Cui, C.5    Sasaki, A.6    Koyama, S.7    Kato, T.8
  • 8
    • 57049151865 scopus 로고    scopus 로고
    • Proteomics analysis identifies phosphorylation-dependent alpha-synuclein protein interactions
    • McFarland, M. A., Ellis, C. E., Markey, S. P., and Nussbaum, R. L. (2008) Proteomics analysis identifies phosphorylation-dependent 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
  • 10
    • 84887510168 scopus 로고    scopus 로고
    • In vivo modulation of polo-like kinases supports a key role for PLK2 in Ser129 alpha-synuclein phosphorylation in mouse brain
    • Bergeron, M., Motter, R., Tanaka, P., Fauss, D., Babcock, M., Chiou, S. S., Nelson, S., San Pablo, F., and Anderson, J. P. (2014) In vivo modulation of polo-like kinases supports a key role for PLK2 in Ser129 alpha-synuclein phosphorylation in mouse brain. Neuroscience 256, 72-82.
    • (2014) Neuroscience , vol.256 , pp. 72-82
    • Bergeron, M.1    Motter, R.2    Tanaka, P.3    Fauss, D.4    Babcock, M.5    Chiou, S.S.6    Nelson, S.7    San Pablo, F.8    Anderson, J.P.9
  • 15
    • 43249108653 scopus 로고    scopus 로고
    • Specificity and regulation of casein kinase-mediated phosphorylation of alphasynuclein
    • Waxman, E. A., and Giasson, B. I. (2008) Specificity and regulation of casein kinase-mediated phosphorylation of alphasynuclein. J. Neuropathol. Exp. Neurol. 67, 402-416.
    • (2008) J. Neuropathol. Exp. Neurol. , vol.67 , pp. 402-416
    • Waxman, E.A.1    Giasson, B.I.2
  • 17
    • 84901364520 scopus 로고    scopus 로고
    • Protein phosphorylation in neurodegeneration: Friend or foe?
    • Tenreiro, S., Eckermann, K., and Outeiro, T. F. (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
  • 18
    • 84864741214 scopus 로고    scopus 로고
    • Phosphorylation of alpha-synuclein is crucial in compensating for proteasomal dysfunction
    • Choi, H. S., Liew, H., Jang, A., Kim, Y. M., Lashuel, H., and Suh, Y. H. (2012) Phosphorylation of alpha-synuclein is crucial in compensating for proteasomal dysfunction. Biochem. Biophys. Res. Commun. 424, 597-603.
    • (2012) Biochem. Biophys. Res. Commun. , vol.424 , pp. 597-603
    • Choi, H.S.1    Liew, H.2    Jang, A.3    Kim, Y.M.4    Lashuel, H.5    Suh, Y.H.6
  • 20
    • 0035830913 scopus 로고    scopus 로고
    • alpha-synuclein is phosphorylated by members of the Src family of protein-tyrosine kinases
    • Ellis, C. E., Schwartzberg, P. L., Grider, T. L., Fink, D. W., and Nussbaum, R. L. (2001) alpha-synuclein is phosphorylated by members of the Src family of protein-tyrosine kinases. J. Biol. Chem. 276, 3879-3884.
    • (2001) J. Biol. Chem. , vol.276 , pp. 3879-3884
    • Ellis, C.E.1    Schwartzberg, P.L.2    Grider, T.L.3    Fink, D.W.4    Nussbaum, R.L.5
  • 22
    • 0036484302 scopus 로고    scopus 로고
    • Multiple phosphorylation of alpha-synuclein by protein tyrosine kinase Syk prevents eosin-induced aggregation
    • Negro, A., Brunati, A. M., Donella-Deana, A., Massimino, M. L., and Pinna, L. A. (2002) Multiple phosphorylation of alpha-synuclein by protein tyrosine kinase Syk prevents eosin-induced aggregation. FASEB J. 16, 210-212.
    • (2002) FASEB J. , vol.16 , pp. 210-212
    • Negro, A.1    Brunati, A.M.2    Donella-Deana, A.3    Massimino, M.L.4    Pinna, L.A.5
  • 23
    • 84890574796 scopus 로고    scopus 로고
    • Alpha-synuclein post-translational modifications as potential biomarkers for Parkinson's disease and other synucleinopathies
    • Schmid, A. W., Fauvet, B., Moniatte, M., and Lashuel, H. A. (2013) Alpha-synuclein post-translational modifications as potential biomarkers for Parkinson's disease and other synucleinopathies. Mol. Cell Proteomics 12, 3543-3558.
    • (2013) Mol. Cell Proteomics , vol.12 , pp. 3543-3558
    • Schmid, A.W.1    Fauvet, B.2    Moniatte, M.3    Lashuel, H.A.4
  • 24
    • 84886779808 scopus 로고    scopus 로고
    • Site-specific NMR mapping and time-resolved monitoring of serine and threonine phosphorylation in reconstituted kinase reactions and mammalian cell extracts
    • Theillet, F. X., Rose, H. M., Liokatis, S., Binolfi, A., Thongwichian, R., Stuiver, M., and Selenko, P. (2013) Site-specific NMR mapping and time-resolved monitoring of serine and threonine phosphorylation in reconstituted kinase reactions and mammalian cell extracts. Nat. Protoc. 8, 1416-1432.
    • (2013) Nat. Protoc. , vol.8 , pp. 1416-1432
    • Theillet, F.X.1    Rose, H.M.2    Liokatis, S.3    Binolfi, A.4    Thongwichian, R.5    Stuiver, M.6    Selenko, P.7
  • 26
    • 84865249504 scopus 로고    scopus 로고
    • Characterization of semi-synthetic and naturally Nalpha-acetylated alpha-synuclein in vitro and in intact cells: Implications for aggregation and cellular properties of alpha-synuclein
    • Fauvet, B., Fares, M. B., Samuel, F., Dikiy, I., Tandon, A., Eliezer, D., and Lashuel, H. A. (2012) Characterization of semi-synthetic 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
  • 30
    • 0025074778 scopus 로고
    • Phosphate groups as substrate determinants for casein kinase I action
    • Flotow, H., Graves, P. R., Wang, A. Q., Fiol, C. J., Roeske, R. W., and Roach, P. J. (1990) Phosphate groups as substrate determinants for casein kinase I action. J. Biol. Chem. 265, 14264-14269.
    • (1990) J. Biol. Chem. , vol.265 , pp. 14264-14269
    • Flotow, H.1    Graves, P.R.2    Wang, A.Q.3    Fiol, C.J.4    Roeske, R.W.5    Roach, P.J.6
  • 31
    • 0025801732 scopus 로고
    • A synthetic beta-casein phosphopeptide and analogues as model substrates for casein kinase-1, a ubiquitous, phosphate directed protein kinase
    • Meggio, F., Perich, J. W., Reynolds, E. C., and Pinna, L. A. (1991) A synthetic beta-casein phosphopeptide and analogues as model substrates for casein kinase-1, a ubiquitous, phosphate directed protein kinase. FEBS Lett. 283, 303-306.
    • (1991) FEBS Lett. , vol.283 , pp. 303-306
    • Meggio, F.1    Perich, J.W.2    Reynolds, E.C.3    Pinna, L.A.4
  • 32
    • 1242276189 scopus 로고    scopus 로고
    • D4476, a cell-permeant inhibitor of CK1, suppresses the site-specific phosphorylation and nuclear exclusion of FOXO1a
    • Rena, G., Bain, J., Elliott, M., and Cohen, P. (2004) D4476, a cell-permeant inhibitor of CK1, suppresses the site-specific phosphorylation and nuclear exclusion of FOXO1a. EMBO Rep. 5, 60-65.
    • (2004) EMBO Rep. , vol.5 , pp. 60-65
    • Rena, G.1    Bain, J.2    Elliott, M.3    Cohen, P.4
  • 33
    • 0026587028 scopus 로고
    • The comparative efficiencies of the Ser(P)-, Thr(P)- and Tyr(P)-residues as specificity determinants for casein kinase-1
    • Meggio, F., Perich, J. W., Marin, O., and Pinna, L. A. (1992) The comparative efficiencies of the Ser(P)-, Thr(P)- and Tyr(P)-residues as specificity determinants for casein kinase-1. Biochem. Biophys. Res. Commun. 182, 1460-1465.
    • (1992) Biochem. Biophys. Res. Commun. , vol.182 , pp. 1460-1465
    • Meggio, F.1    Perich, J.W.2    Marin, O.3    Pinna, L.A.4
  • 34
    • 13844294211 scopus 로고    scopus 로고
    • The casein kinase 1 family: Participation in multiple cellular processes in eukaryotes
    • Knippschild, U., Gocht, A., Wolff, S., Huber, N., Lohler, J., and Stoter, M. (2005) The casein kinase 1 family: Participation in multiple cellular processes in eukaryotes. Cell. Signalling 17, 675-689.
    • (2005) Cell. Signalling , vol.17 , pp. 675-689
    • Knippschild, U.1    Gocht, A.2    Wolff, S.3    Huber, N.4    Lohler, J.5    Stoter, M.6
  • 36
    • 0035066885 scopus 로고    scopus 로고
    • Direct binding and functional coupling of alpha-synuclein to the dopamine transporters accelerate dopamine-induced apoptosis
    • Lee, F. J., Liu, F., Pristupa, Z. B., and Niznik, H. B. (2001) Direct binding and functional coupling of alpha-synuclein to the dopamine transporters accelerate dopamine-induced apoptosis. FASEB J. 15, 916-926.
    • (2001) FASEB J. , vol.15 , pp. 916-926
    • Lee, F.J.1    Liu, F.2    Pristupa, Z.B.3    Niznik, H.B.4
  • 37
    • 30844456535 scopus 로고    scopus 로고
    • SOFAST-HMQC experiments for recording two-dimensional heteronuclear correlation spectra of proteins within a few seconds
    • Schanda, P., Kupce, E., and Brutscher, B. (2005) SOFAST-HMQC experiments for recording two-dimensional heteronuclear correlation spectra of proteins within a few seconds. J. Biomol. NMR 33, 199-211.
    • (2005) J. Biomol. NMR , vol.33 , pp. 199-211
    • Schanda, P.1    Kupce, E.2    Brutscher, B.3
  • 38
    • 49249127687 scopus 로고    scopus 로고
    • Polo-like kinase 3 functions as a tumor suppressor and is a negative regulator of hypoxia-inducible factor-1 alpha under hypoxic conditions
    • Yang, Y., Bai, J., Shen, R., Brown, S. A., Komissarova, E., Huang, Y., Jiang, N., Alberts, G. F., Costa, M., Lu, L., Winkles, J. A., and Dai, W. (2008) Polo-like kinase 3 functions as a tumor suppressor and is a negative regulator of hypoxia-inducible factor-1 alpha under hypoxic conditions. Cancer Res. 68, 4077-4085.
    • (2008) Cancer Res. , vol.68 , pp. 4077-4085
    • Yang, Y.1    Bai, J.2    Shen, R.3    Brown, S.A.4    Komissarova, E.5    Huang, Y.6    Jiang, N.7    Alberts, G.F.8    Costa, M.9    Lu, L.10    Winkles, J.A.11    Dai, W.12


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.