Phosphorylation of α-synuclein protein at Ser-129 reduces neuronal dysfunction by lowering its membrane binding property in Caenorhabditis elegans.

@article{Kuwahara2012PhosphorylationO,
  title={Phosphorylation of α-synuclein protein at Ser-129 reduces neuronal dysfunction by lowering its membrane binding property in Caenorhabditis elegans.},
  author={Tomoki Kuwahara and Reina Tonegawa and Genta Ito and Shohei Mitani and Takeshi Iwatsubo},
  journal={The Journal of biological chemistry},
  year={2012},
  volume={287 10},
  pages={7098-109}
}
α-Synuclein is causative for autosomal dominant familial Parkinson disease and dementia with Lewy bodies, and the phosphorylation of α-synuclein at residue Ser-129 is a key posttranslational modification detected in Parkinson disease/dementia with Lewy bodies lesions. However, the role of Ser-129 phosphorylation on the pathogenesis of Parkinson disease/dementia with Lewy bodies remains unclear. Here we investigated the neurotoxicity of Ser-129-substituted α-synuclein in the transgenic… CONTINUE READING