Co-association of parkin and α-synuclein

Peter Choi, Natalie Golts, Heather Snyder, Matthew Chong, Leonard Petrucelli, John Hardy, Dennis Sparkman, Elizabeth Cochran, Jack M. Lee, Benjamin Wolozin

Research output: Contribution to journalArticlepeer-review

62 Scopus citations


Parkin and α-synuclein are two proteins that are associated with the pathophysiology of Parkinson's disease (PD). Parkin is present in Lewy bodies and axonal spheroids in brains affected by PD, and mutations in parkin cause hereditary forms of Parkinsonism. α-Synuclein is a major component of Lewy bodies and is associated with rare cases of PD. We now show that parkin binds to α-synuclein, including conditions associated with α-synuclein aggregation. Parkin and α-synuclein complexes were observed in BE-M17 cells under basal conditions, in BE-M17 cells under oxidative conditions and in brains from control or PD donors. Double staining of PD brains shows parkin and α-synuclein co-localize to the same pathological structures (both Lewy bodies and axonal spheroids). These results suggest that parkin interacts with α-synuclein and could contribute to the pathophysiology of PD more generally than was previously considered.

Original languageEnglish (US)
Pages (from-to)2839-2843
Number of pages5
Issue number13
StatePublished - Sep 17 2001


  • Aggregation
  • Chaperone
  • Immunoprecipitation
  • Lewy body
  • Pathology
  • Ubiquitination

ASJC Scopus subject areas

  • General Neuroscience


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