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http://purl.uniprot.org/citations/22851696http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22851696http://www.w3.org/2000/01/rdf-schema#comment"Interleukin-17 (IL-17) is critically involved in the pathogenesis of various inflammatory disorders. IL-17 receptor (IL-17R)-proximal signaling complex (IL-17R-Act1-TRAF6) is essential for IL-17-mediated NF-κB activation, while IL-17-mediated mRNA stability is TRAF6 independent. Recently, inducible IκB kinase (IKKi) has been shown to phosphorylate Act1 on Ser 311 to mediate IL-17-induced mRNA stability. Here we show that TANK binding kinase 1 (TBK1), the other IKK-related kinase, directly phosphorylated Act1 on three other Ser sites to suppress IL-17R-mediated NF-κB activation. IL-17 stimulation activated TBK1 and induced its association with Act1. IKKi also phosphorylated Act1 on the three serine sites and played a redundant role with TBK1 in suppressing IL-17-induced NF-κB activation. Act1 phosphorylation on the three sites inhibited its association with TRAF6 and consequently NF-κB activation in IL-17R signaling. Interestingly, TRAF6, but not TRAF3, which is the upstream adaptor of the IKK-related kinases in antiviral signaling, was critical for IL-17-induced Act1 phosphorylation. TRAF6 was essential for IL-17-induced TBK1 activation, its association with Act1, and consequent Act1 phosphorylation. Our findings define a new role for the IKK-related kinases in suppressing IL-17-mediated NF-κB activation through TRAF6-dependent Act1 phosphorylation."xsd:string
http://purl.uniprot.org/citations/22851696http://purl.org/dc/terms/identifier"doi:10.1128/mcb.00268-12"xsd:string
http://purl.uniprot.org/citations/22851696http://purl.uniprot.org/core/author"Gao H."xsd:string
http://purl.uniprot.org/citations/22851696http://purl.uniprot.org/core/author"Liu Y."xsd:string
http://purl.uniprot.org/citations/22851696http://purl.uniprot.org/core/author"Qian Y."xsd:string
http://purl.uniprot.org/citations/22851696http://purl.uniprot.org/core/author"Shi Y."xsd:string
http://purl.uniprot.org/citations/22851696http://purl.uniprot.org/core/author"Zhang Y."xsd:string
http://purl.uniprot.org/citations/22851696http://purl.uniprot.org/core/author"Yao Y."xsd:string
http://purl.uniprot.org/citations/22851696http://purl.uniprot.org/core/author"Zhu S."xsd:string
http://purl.uniprot.org/citations/22851696http://purl.uniprot.org/core/author"Qu F."xsd:string
http://purl.uniprot.org/citations/22851696http://purl.uniprot.org/core/author"Shi P."xsd:string
http://purl.uniprot.org/citations/22851696http://purl.uniprot.org/core/author"Jallal B."xsd:string
http://purl.uniprot.org/citations/22851696http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/22851696http://purl.uniprot.org/core/name"Mol Cell Biol"xsd:string
http://purl.uniprot.org/citations/22851696http://purl.uniprot.org/core/pages"3925-3937"xsd:string
http://purl.uniprot.org/citations/22851696http://purl.uniprot.org/core/title"TRAF6-dependent Act1 phosphorylation by the IkappaB kinase-related kinases suppresses interleukin-17-induced NF-kappaB activation."xsd:string
http://purl.uniprot.org/citations/22851696http://purl.uniprot.org/core/volume"32"xsd:string
http://purl.uniprot.org/citations/22851696http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/22851696
http://purl.uniprot.org/citations/22851696http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/22851696
http://purl.uniprot.org/uniprot/#_A0A0G2JGK6-mappedCitation-22851696http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/22851696
http://purl.uniprot.org/uniprot/#_E0CY50-mappedCitation-22851696http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/22851696
http://purl.uniprot.org/uniprot/#_A1L361-mappedCitation-22851696http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/22851696
http://purl.uniprot.org/uniprot/#_A0A1W2P835-mappedCitation-22851696http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/22851696
http://purl.uniprot.org/uniprot/#_A0A510GAH8-mappedCitation-22851696http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/22851696