Serine 129 Phosphorylation Reduces Α-synuclein’s Ability to Regulate Tyrosine Hydroxylase and Protein Phosphatase 2a in Vitro and in Vivo
نویسندگان
چکیده
SERINE 129 PHOSPHORYLATION REDUCES α-SYNUCLEIN’S ABILITY TO REGULATE TYROSINE HYDROXYLASE AND PROTEIN PHOSPHATASE 2A IN VITRO AND IN VIVO Haiyan Lou*, Susana E. Montoya*, Tshianda N. M. Alerte*, Jian Wang, Jianjun Wu, Xiangmin Peng, Chang-Sook Hong, Emily E. Friedrich, Samantha A. Mader, Courtney J. Pedersen, Brian S. Marcus, Alison L. McCormack, Donato A. Di Monte, S. Colette Daubner, Ruth G. Perez 5, 6 Pittsburgh Institute for Neurodegenerative Diseases, University of Pittsburgh, Pittsburgh, PA, 15261, USA; Department of Pharmacology, Shandong University School of Medicine, Jinan, Shandong, 250012, P. R. China; The Parkinson’s Institute, Sunnyvale, CA 94085, USA; Department of Biological Sciences, St. Mary’s University, San Antonio, TX, 78229, USA. Department of Neurology, and Department of Pharmacology & Chemical Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA, 15261, USA
منابع مشابه
Serine 129 Phosphorylation Reduces the Ability of α-Synuclein to Regulate Tyrosine Hydroxylase and Protein Phosphatase 2A in Vitro and in Vivo*
Alpha-synuclein (a-Syn), a protein implicated in Parkinson disease, contributes significantly to dopamine metabolism. a-Syn binding inhibits the activity of tyrosine hydroxylase (TH), the rate-limiting enzyme in catecholamine synthesis. Phosphorylation of TH stimulates its activity, an effect that is reversed by protein phosphatase 2A (PP2A). In cells, a-Syn overexpression activates PP2A. Here ...
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α-Synuclein (α-Syn) is a key protein that accumulates as hyperphosphorylated aggregates in pathologic hallmark features of Parkinson's disease (PD) and other neurodegenerative disorders. Phosphorylation of this protein at serine 129 is believed to promote its aggregation and neurotoxicity, suggesting that this post-translational modification could be a therapeutic target. Here, we demonstrate t...
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