RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/21778237http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21778237http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21778237http://www.w3.org/2000/01/rdf-schema#comment"Cullin RING ligases (CRLs), the most prolific class of ubiquitin ligase enzymes, are multimeric complexes that regulate a wide range of cellular processes. CRL activity is regulated by CAND1 (Cullin-associated Nedd8-dissociated protein 1), an inhibitor that promotes the dissociation of substrate receptor components from the CRL. We demonstrate here that COMMD1 (copper metabolism MURR1 domain-containing 1), a factor previously found to promote ubiquitination of various substrates, regulates CRL activation by antagonizing CAND1 binding. We show that COMMD1 interacts with multiple Cullins, that the COMMD1-Cul2 complex cannot bind CAND1, and that, conversely, COMMD1 can actively displace CAND1 from CRLs. These findings highlight a novel mechanism of CRL activation and suggest that CRL regulation may underlie the pleiotropic activities of COMMD1."xsd:string
http://purl.uniprot.org/citations/21778237http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m111.278408"xsd:string
http://purl.uniprot.org/citations/21778237http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m111.278408"xsd:string
http://purl.uniprot.org/citations/21778237http://purl.uniprot.org/core/author"Chen B."xsd:string
http://purl.uniprot.org/citations/21778237http://purl.uniprot.org/core/author"Chen B."xsd:string
http://purl.uniprot.org/citations/21778237http://purl.uniprot.org/core/author"Li H."xsd:string
http://purl.uniprot.org/citations/21778237http://purl.uniprot.org/core/author"Li H."xsd:string
http://purl.uniprot.org/citations/21778237http://purl.uniprot.org/core/author"Mao X."xsd:string
http://purl.uniprot.org/citations/21778237http://purl.uniprot.org/core/author"Mao X."xsd:string
http://purl.uniprot.org/citations/21778237http://purl.uniprot.org/core/author"Burstein E."xsd:string
http://purl.uniprot.org/citations/21778237http://purl.uniprot.org/core/author"Burstein E."xsd:string
http://purl.uniprot.org/citations/21778237http://purl.uniprot.org/core/author"Gluck N."xsd:string
http://purl.uniprot.org/citations/21778237http://purl.uniprot.org/core/author"Gluck N."xsd:string
http://purl.uniprot.org/citations/21778237http://purl.uniprot.org/core/author"Maine G.N."xsd:string
http://purl.uniprot.org/citations/21778237http://purl.uniprot.org/core/author"Maine G.N."xsd:string
http://purl.uniprot.org/citations/21778237http://purl.uniprot.org/core/author"Starokadomskyy P."xsd:string
http://purl.uniprot.org/citations/21778237http://purl.uniprot.org/core/author"Starokadomskyy P."xsd:string
http://purl.uniprot.org/citations/21778237http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/21778237http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/21778237http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/21778237http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/21778237http://purl.uniprot.org/core/pages"32355-32365"xsd:string
http://purl.uniprot.org/citations/21778237http://purl.uniprot.org/core/pages"32355-32365"xsd:string