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Title: Parkin occurs in a stable, non-covalent, approximately 110-kDa complex in brain
Authors: Van Humbeeck, Cindy ×
Waelkens, Etienne
Corti, Olga
Brice, Alexis
Vandenberghe, Wim #
Issue Date: Jan-2008
Publisher: Published on behalf of the European Neuroscience Association by Oxford University Press
Series Title: European Journal of Neuroscience vol:27 issue:2 pages: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.
URI: 
ISSN: 0953-816X
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Research Group Experimental Neurology
Biochemistry Section (Medicine) (-)
Laboratory for Parkinson Research
Laboratory of Protein Phosphorylation and Proteomics
Laboratory of Phosphoproteomics (-)
× corresponding author
# (joint) last author

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