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http://purl.uniprot.org/citations/20551172http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20551172http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20551172http://www.w3.org/2000/01/rdf-schema#comment"Rapid Myc protein turnover is critical for maintaining basal levels of Myc activity in normal cells and a prompt response to changing growth signals. We characterize a new Myc-interacting factor, TRPC4AP (transient receptor potential cation channel, subfamily C, member 4-associated protein)/TRUSS (tumor necrosis factor receptor-associated ubiquitous scaffolding and signaling protein), which is the receptor for a DDB1 (damage-specific DNA-binding protein 1)-CUL4 (Cullin 4) E3 ligase complex for selective Myc degradation through the proteasome. TRPC4AP/TRUSS binds specifically to the Myc C terminus and promotes its ubiquitination and destruction through the recognition of evolutionarily conserved domains in the Myc N terminus. TRPC4AP/TRUSS suppresses Myc-mediated transactivation and transformation in a dose-dependent manner. Finally, we found that TRPC4AP/TRUSS expression is strongly down-regulated in most cancer cell lines, leading to Myc protein stabilization. These studies identify a novel pathway targeting Myc degradation that is suppressed in cancer cells."xsd:string
http://purl.uniprot.org/citations/20551172http://purl.org/dc/terms/identifier"doi:10.1101/gad.1920310"xsd:string
http://purl.uniprot.org/citations/20551172http://purl.org/dc/terms/identifier"doi:10.1101/gad.1920310"xsd:string
http://purl.uniprot.org/citations/20551172http://purl.uniprot.org/core/author"Gerber S.A."xsd:string
http://purl.uniprot.org/citations/20551172http://purl.uniprot.org/core/author"Gerber S.A."xsd:string
http://purl.uniprot.org/citations/20551172http://purl.uniprot.org/core/author"Choi S.H."xsd:string
http://purl.uniprot.org/citations/20551172http://purl.uniprot.org/core/author"Choi S.H."xsd:string
http://purl.uniprot.org/citations/20551172http://purl.uniprot.org/core/author"Cole M.D."xsd:string
http://purl.uniprot.org/citations/20551172http://purl.uniprot.org/core/author"Cole M.D."xsd:string
http://purl.uniprot.org/citations/20551172http://purl.uniprot.org/core/author"Wright J.B."xsd:string
http://purl.uniprot.org/citations/20551172http://purl.uniprot.org/core/author"Wright J.B."xsd:string
http://purl.uniprot.org/citations/20551172http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20551172http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20551172http://purl.uniprot.org/core/name"Genes Dev."xsd:string
http://purl.uniprot.org/citations/20551172http://purl.uniprot.org/core/name"Genes Dev."xsd:string
http://purl.uniprot.org/citations/20551172http://purl.uniprot.org/core/pages"1236-1241"xsd:string
http://purl.uniprot.org/citations/20551172http://purl.uniprot.org/core/pages"1236-1241"xsd:string
http://purl.uniprot.org/citations/20551172http://purl.uniprot.org/core/title"Myc protein is stabilized by suppression of a novel E3 ligase complex in cancer cells."xsd:string
http://purl.uniprot.org/citations/20551172http://purl.uniprot.org/core/title"Myc protein is stabilized by suppression of a novel E3 ligase complex in cancer cells."xsd:string
http://purl.uniprot.org/citations/20551172http://purl.uniprot.org/core/volume"24"xsd:string
http://purl.uniprot.org/citations/20551172http://purl.uniprot.org/core/volume"24"xsd:string
http://purl.uniprot.org/citations/20551172http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/20551172
http://purl.uniprot.org/citations/20551172http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/20551172