Serine 129 Phosphorylation Reduces the Ability of α-Synuclein to Regulate Tyrosine Hydroxylase and Protein Phosphatase 2A in Vitro and in Vivo*

@inproceedings{Lou2010Serine1P,
  title={Serine 129 Phosphorylation Reduces the Ability of α-Synuclein to Regulate Tyrosine Hydroxylase and Protein Phosphatase 2A in Vitro and in Vivo*},
  author={Haiyan Lou and Susana E. Montoya and Tshianda N. M. Alerte and Jian Wang and Jianjun Wu and Xiangmin Peng and C F Hong and Emily E Friedrich and Samantha Ann Mader and Courtney J. Pedersen and Brian S. Marcus and Alison L. McCormack and Donato A. Di Monte and Simon Daubner and Ruth G. Perez},
  booktitle={The Journal of biological chemistry},
  year={2010}
}
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 we demonstrate that a-Syn significantly inhibited TH activity in vitro and in vivo and that… CONTINUE READING
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