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http://purl.uniprot.org/citations/15603737http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15603737http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15603737http://www.w3.org/2000/01/rdf-schema#comment"Loss-of-function mutations in the parkin gene, which encodes an E3 ubiquitin ligase, are the major cause of early-onset Parkinson's disease (PD). Decreases in parkin activity may also contribute to neurodegeneration in sporadic forms of PD. Here, we show that bcl-2-associated athanogene 5 (BAG5), a BAG family member, directly interacts with parkin and the chaperone Hsp70. Within this complex, BAG5 inhibits both parkin E3 ubiquitin ligase activity and Hsp70-mediated refolding of misfolded proteins. BAG5 enhances parkin sequestration within protein aggregates and mitigates parkin-dependent preservation of proteasome function. Finally, BAG5 enhances dopamine neuron death in an in vivo model of PD, whereas a mutant that inhibits BAG5 activity attenuates dopaminergic neurodegeneration. This contrasts with the antideath functions ascribed to BAG family members and suggests a potential role for BAG5 in promoting neurodegeneration in sporadic PD through its functional interactions with parkin and Hsp70."xsd:string
http://purl.uniprot.org/citations/15603737http://purl.org/dc/terms/identifier"doi:10.1016/j.neuron.2004.11.026"xsd:string
http://purl.uniprot.org/citations/15603737http://purl.org/dc/terms/identifier"doi:10.1016/j.neuron.2004.11.026"xsd:string
http://purl.uniprot.org/citations/15603737http://purl.uniprot.org/core/author"Lee S."xsd:string
http://purl.uniprot.org/citations/15603737http://purl.uniprot.org/core/author"Lee S."xsd:string
http://purl.uniprot.org/citations/15603737http://purl.uniprot.org/core/author"Liu L."xsd:string
http://purl.uniprot.org/citations/15603737http://purl.uniprot.org/core/author"Liu L."xsd:string
http://purl.uniprot.org/citations/15603737http://purl.uniprot.org/core/author"Fon E.A."xsd:string
http://purl.uniprot.org/citations/15603737http://purl.uniprot.org/core/author"Fon E.A."xsd:string
http://purl.uniprot.org/citations/15603737http://purl.uniprot.org/core/author"Park D.S."xsd:string
http://purl.uniprot.org/citations/15603737http://purl.uniprot.org/core/author"Park D.S."xsd:string
http://purl.uniprot.org/citations/15603737http://purl.uniprot.org/core/author"Smith P.D."xsd:string
http://purl.uniprot.org/citations/15603737http://purl.uniprot.org/core/author"Smith P.D."xsd:string
http://purl.uniprot.org/citations/15603737http://purl.uniprot.org/core/author"Crocker S.J."xsd:string
http://purl.uniprot.org/citations/15603737http://purl.uniprot.org/core/author"Crocker S.J."xsd:string
http://purl.uniprot.org/citations/15603737http://purl.uniprot.org/core/author"Glover J.R."xsd:string
http://purl.uniprot.org/citations/15603737http://purl.uniprot.org/core/author"Glover J.R."xsd:string
http://purl.uniprot.org/citations/15603737http://purl.uniprot.org/core/author"Kalia S.K."xsd:string
http://purl.uniprot.org/citations/15603737http://purl.uniprot.org/core/author"Kalia S.K."xsd:string
http://purl.uniprot.org/citations/15603737http://purl.uniprot.org/core/author"Lozano A.M."xsd:string
http://purl.uniprot.org/citations/15603737http://purl.uniprot.org/core/author"Lozano A.M."xsd:string
http://purl.uniprot.org/citations/15603737http://purl.uniprot.org/core/author"Thorarinsdottir T.E."xsd:string
http://purl.uniprot.org/citations/15603737http://purl.uniprot.org/core/author"Thorarinsdottir T.E."xsd:string