RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/15728840http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15728840http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15728840http://www.w3.org/2000/01/rdf-schema#comment"It is widely accepted that the familial Parkinson's disease (PD)-linked gene product, parkin, functions as a ubiquitin ligase involved in protein turnover via the ubiquitin-proteasome system. Substrates ubiquitinated by parkin are hence thought to be destined for proteasomal degradation. Because we demonstrated previously that parkin interacts with and ubiquitinates synphilin-1, we initially expected synphilin-1 degradation to be enhanced in the presence of parkin. Contrary to our expectation, we found that synphilin-1 is normally ubiquitinated by parkin in a nonclassical, proteasomal-independent manner that involves lysine 63 (K63)-linked polyubiquitin chain formation. Parkin-mediated degradation of synphilin-1 occurs appreciably only at an unusually high parkin to synphilin-1 expression ratio or when primed for lysine 48 (K48)-linked ubiquitination. In addition we found that parkin-mediated ubiquitination of proteins within Lewy-body-like inclusions formed by the coexpression of synphilin-1, alpha-synuclein, and parkin occurs predominantly via K63 linkages and that the formation of these inclusions is enhanced by K63-linked ubiquitination. Our results suggest that parkin is a dual-function ubiquitin ligase and that K63-linked ubiquitination of synphilin-1 by parkin may be involved in the formation of Lewy body inclusions associated with PD."xsd:string
http://purl.uniprot.org/citations/15728840http://purl.org/dc/terms/identifier"doi:10.1523/jneurosci.4474-04.2005"xsd:string
http://purl.uniprot.org/citations/15728840http://purl.org/dc/terms/identifier"doi:10.1523/jneurosci.4474-04.2005"xsd:string
http://purl.uniprot.org/citations/15728840http://purl.uniprot.org/core/author"Tanaka Y."xsd:string
http://purl.uniprot.org/citations/15728840http://purl.uniprot.org/core/author"Tanaka Y."xsd:string
http://purl.uniprot.org/citations/15728840http://purl.uniprot.org/core/author"Wang C."xsd:string
http://purl.uniprot.org/citations/15728840http://purl.uniprot.org/core/author"Wang C."xsd:string
http://purl.uniprot.org/citations/15728840http://purl.uniprot.org/core/author"Zhang Y."xsd:string
http://purl.uniprot.org/citations/15728840http://purl.uniprot.org/core/author"Zhang Y."xsd:string
http://purl.uniprot.org/citations/15728840http://purl.uniprot.org/core/author"Ross C.A."xsd:string
http://purl.uniprot.org/citations/15728840http://purl.uniprot.org/core/author"Ross C.A."xsd:string
http://purl.uniprot.org/citations/15728840http://purl.uniprot.org/core/author"Engelender S."xsd:string
http://purl.uniprot.org/citations/15728840http://purl.uniprot.org/core/author"Engelender S."xsd:string
http://purl.uniprot.org/citations/15728840http://purl.uniprot.org/core/author"Lim K.L."xsd:string
http://purl.uniprot.org/citations/15728840http://purl.uniprot.org/core/author"Lim K.L."xsd:string
http://purl.uniprot.org/citations/15728840http://purl.uniprot.org/core/author"Dawson T.M."xsd:string
http://purl.uniprot.org/citations/15728840http://purl.uniprot.org/core/author"Dawson T.M."xsd:string
http://purl.uniprot.org/citations/15728840http://purl.uniprot.org/core/author"Dawson V.L."xsd:string
http://purl.uniprot.org/citations/15728840http://purl.uniprot.org/core/author"Dawson V.L."xsd:string
http://purl.uniprot.org/citations/15728840http://purl.uniprot.org/core/author"Smith W."xsd:string
http://purl.uniprot.org/citations/15728840http://purl.uniprot.org/core/author"Smith W."xsd:string
http://purl.uniprot.org/citations/15728840http://purl.uniprot.org/core/author"Chew K.C."xsd:string
http://purl.uniprot.org/citations/15728840http://purl.uniprot.org/core/author"Chew K.C."xsd:string