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http://purl.uniprot.org/citations/9990853http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9990853http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9990853http://www.w3.org/2000/01/rdf-schema#comment"Signal-induced phosphorylation of IkappaBalpha targets this inhibitor of NF-kappaB for ubiquitination and subsequent degradation, thus allowing NF-kappaB to enter the nucleus to turn on its target genes. We report here the identification of an IkappaB-ubiquitin (Ub) ligase complex containing the F-box/WD40-repeat protein, beta-TrCP, a vertebrate homolog of Drosophila Slimb. beta-TrCP binds to IkappaBalpha only when the latter is specifically phosphorylated by an IkappaB kinase complex. Moreover, immunopurified beta-TrCP ubiquitinates phosphorylated IkappaBalpha at specific lysines in the presence of Ub-activating (E1) and -conjugating (Ubch5) enzymes. A beta-TrCP mutant lacking the F-box inhibits the signal-induced degradation of IkappaBalpha and subsequent activation of NF-kappaB-dependent transcription. Furthermore, Drosophila embryos deficient in slimb fail to activate twist and snail, two genes known to be regulated by the NF-kappaB homolog, Dorsal. These biochemical and genetic data strongly suggest that Slimb/beta-TrCP is the specificity determinant for the signal-induced ubiquitination of IkappaBalpha."xsd:string
http://purl.uniprot.org/citations/9990853http://purl.org/dc/terms/identifier"doi:10.1101/gad.13.3.284"xsd:string
http://purl.uniprot.org/citations/9990853http://purl.org/dc/terms/identifier"doi:10.1101/gad.13.3.284"xsd:string
http://purl.uniprot.org/citations/9990853http://purl.uniprot.org/core/author"Jiang J."xsd:string
http://purl.uniprot.org/citations/9990853http://purl.uniprot.org/core/author"Jiang J."xsd:string
http://purl.uniprot.org/citations/9990853http://purl.uniprot.org/core/author"Chen Z.J."xsd:string
http://purl.uniprot.org/citations/9990853http://purl.uniprot.org/core/author"Chen Z.J."xsd:string
http://purl.uniprot.org/citations/9990853http://purl.uniprot.org/core/author"Spencer E."xsd:string
http://purl.uniprot.org/citations/9990853http://purl.uniprot.org/core/author"Spencer E."xsd:string
http://purl.uniprot.org/citations/9990853http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/9990853http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/9990853http://purl.uniprot.org/core/name"Genes Dev."xsd:string
http://purl.uniprot.org/citations/9990853http://purl.uniprot.org/core/name"Genes Dev."xsd:string
http://purl.uniprot.org/citations/9990853http://purl.uniprot.org/core/pages"284-294"xsd:string
http://purl.uniprot.org/citations/9990853http://purl.uniprot.org/core/pages"284-294"xsd:string
http://purl.uniprot.org/citations/9990853http://purl.uniprot.org/core/title"Signal-induced ubiquitination of IkappaBalpha by the F-box protein Slimb/beta-TrCP."xsd:string
http://purl.uniprot.org/citations/9990853http://purl.uniprot.org/core/title"Signal-induced ubiquitination of IkappaBalpha by the F-box protein Slimb/beta-TrCP."xsd:string
http://purl.uniprot.org/citations/9990853http://purl.uniprot.org/core/volume"13"xsd:string
http://purl.uniprot.org/citations/9990853http://purl.uniprot.org/core/volume"13"xsd:string
http://purl.uniprot.org/citations/9990853http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9990853
http://purl.uniprot.org/citations/9990853http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9990853
http://purl.uniprot.org/citations/9990853http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9990853
http://purl.uniprot.org/citations/9990853http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9990853