PMID:18190519

Citation	Van Humbeeck, C, Waelkens, E, Corti, O, Brice, A and Vandenberghe, W (2008) Parkin occurs in a stable, non-covalent, approximately 110-kDa complex in brain. Eur. J. Neurosci. 27:284-93
Abstract	Mutations in the gene for parkin, a 52-kDa E3 ubiquitin ligase, are a major cause of hereditary Parkinson's disease (PD). In vitro studies have identified a large number of parkin-interacting proteins. Whether parkin exists as a monomer or as part of a stable protein complex in vivo is uncertain. Here we demonstrate that endogenous parkin occurs in a stable, non-covalent, approximately 110-kDa complex in native extracts from mouse brain, heart and skeletal muscle, while monomeric parkin is undetectable. Partial denaturation experiments indicate that this complex is at least a tetramer. Reported parkin-binding partners do not show detectable association with the parkin complex on native gels. Upon overexpression in COS1, SH-SY5Y or CHO cells, parkin accumulates predominantly as a monomer, suggesting that the interactors required for complex formation are available in limiting amounts in these cells. Importantly, PD-linked parkin mutations significantly impair parkin complex formation. These data demonstrate that parkin oligomerizes into a stable, non-covalent, heteromeric complex in vivo, and suggest that parkin may have as yet unidentified stable binding partners.
Links	PubMed PMC2253705 Online version:10.1111/j.1460-9568.2007.06000.x
Keywords	Animals; Brain/metabolism; Brain Chemistry/physiology; CHO Cells; COS Cells; Cercopithecus aethiops; Cricetinae; Cricetulus; Humans; Mice; Mice, Inbred C57BL; Mice, Knockout; Ubiquitin-Protein Ligases/analysis; Ubiquitin-Protein Ligases/biosynthesis; Ubiquitin-Protein Ligases/genetics
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