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http://purl.uniprot.org/citations/17449468http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17449468http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17449468http://www.w3.org/2000/01/rdf-schema#comment"Inflammation is a homeostatic mechanism that limits the effects of infectious agents. Tumor necrosis factor (TNF) and interleukin (IL)-1 are two cytokines that induce inflammation through activation of the transcription factor NF-kappaB. Various studies have suggested that two homologous and structurally related adapter proteins TAB2 and TAB3 play redundant roles in TNF- and IL-1-mediated NF-kappaB activation pathways. Both TAB2 and TAB3 contain CUE, coiled-coil, and nuclear protein localization 4 zinc finger (NZF) domains. The NZF domains of TAB2/3 are critical for TAB2/3 to bind to Lys(63)-linked polyubiquitin chains of other adaptor proteins, such as receptor-interacting protein and TRAF6, which are two signaling proteins essential for TNF- and IL-1-induced NF-kappaB activation, respectively. In a search for proteins containing NZF domains conserved with those of TAB2/3, we identified RBCK1, which has been shown to act as an E3 ubiquitin ligase in iron metabolism. Overexpression of RBCK1 negatively regulates TAB2/3-mediated and TNF- and IL-1-induced NF-kappaB activation, whereas knockdown of RBCK1 by RNA interference potentiates TNF- and IL-1-induced NF-kappaB activation. RBCK1 physically interacts with TAB2/3 and facilitates degradation of TAB2/3 through a proteasome-dependent process. Taken together, our findings suggest that RBCK1 is involved in negative regulation of inflammatory signaling triggered by TNF and IL-1 through targeting TAB2/3 for degradation."xsd:string
http://purl.uniprot.org/citations/17449468http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m701913200"xsd:string
http://purl.uniprot.org/citations/17449468http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m701913200"xsd:string
http://purl.uniprot.org/citations/17449468http://purl.uniprot.org/core/author"Tian Y."xsd:string
http://purl.uniprot.org/citations/17449468http://purl.uniprot.org/core/author"Tian Y."xsd:string
http://purl.uniprot.org/citations/17449468http://purl.uniprot.org/core/author"Zhang Y."xsd:string
http://purl.uniprot.org/citations/17449468http://purl.uniprot.org/core/author"Zhang Y."xsd:string
http://purl.uniprot.org/citations/17449468http://purl.uniprot.org/core/author"Zhang M."xsd:string
http://purl.uniprot.org/citations/17449468http://purl.uniprot.org/core/author"Zhang M."xsd:string
http://purl.uniprot.org/citations/17449468http://purl.uniprot.org/core/author"Zhong B."xsd:string
http://purl.uniprot.org/citations/17449468http://purl.uniprot.org/core/author"Zhong B."xsd:string
http://purl.uniprot.org/citations/17449468http://purl.uniprot.org/core/author"Wang Y.Y."xsd:string
http://purl.uniprot.org/citations/17449468http://purl.uniprot.org/core/author"Wang Y.Y."xsd:string
http://purl.uniprot.org/citations/17449468http://purl.uniprot.org/core/author"Wang R.P."xsd:string
http://purl.uniprot.org/citations/17449468http://purl.uniprot.org/core/author"Wang R.P."xsd:string
http://purl.uniprot.org/citations/17449468http://purl.uniprot.org/core/author"Chen D.Y."xsd:string
http://purl.uniprot.org/citations/17449468http://purl.uniprot.org/core/author"Chen D.Y."xsd:string
http://purl.uniprot.org/citations/17449468http://purl.uniprot.org/core/author"Shu H.B."xsd:string
http://purl.uniprot.org/citations/17449468http://purl.uniprot.org/core/author"Shu H.B."xsd:string
http://purl.uniprot.org/citations/17449468http://purl.uniprot.org/core/author"Zhai Z.H."xsd:string
http://purl.uniprot.org/citations/17449468http://purl.uniprot.org/core/author"Zhai Z.H."xsd:string
http://purl.uniprot.org/citations/17449468http://purl.uniprot.org/core/author"Diao F.C."xsd:string
http://purl.uniprot.org/citations/17449468http://purl.uniprot.org/core/author"Diao F.C."xsd:string