α-Synuclein Shows High Affinity Interaction with Voltage-dependent Anion Channel, Suggesting Mechanisms of Mitochondrial Regulation and Toxicity in Parkinson Disease.

@article{Rostovtseva2015SynucleinSH,
  title={α-Synuclein Shows High Affinity Interaction with Voltage-dependent Anion Channel, Suggesting Mechanisms of Mitochondrial Regulation and Toxicity in Parkinson Disease.},
  author={Tatiana K. Rostovtseva and Philip A. Gurnev and Olga Protchenko and David P. Hoogerheide and Thai Leong Yap and Caroline C. Philpott and Jennifer C Lee and Sergey M. Bezrukov},
  journal={The Journal of biological chemistry},
  year={2015},
  volume={290 30},
  pages={18467-77}
}
Participation of the small, intrinsically disordered protein α-synuclein (α-syn) in Parkinson disease (PD) pathogenesis has been well documented. Although recent research demonstrates the involvement of α-syn in mitochondrial dysfunction in neurodegeneration and suggests direct interaction of α-syn with mitochondria, the molecular mechanism(s) of α-syn toxicity and its effect on neuronal mitochondria remain vague. Here we report that at nanomolar concentrations, α-syn reversibly blocks the… CONTINUE READING

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