{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Lamothe B"],"funding":["NIAID NIH HHS","NCI NIH HHS","NIAMS NIH HHS"],"pagination":["4102-12"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3221607"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["282(6)"],"pubmed_abstract":["Tumor necrosis factor (TNF) receptor-associated factor 6 (TRAF6) is a key mediator in proximal signaling of the interleukin-1/Toll-like receptor and the TNF receptor superfamily. Analysis of TRAF6-deficient mice revealed a fundamental role of TRAF6 in osteoclastogenesis; however, the molecular mechanism underlying TRAF6 signaling in this biological process is not understood. Recent biochemical evidence has indicated that TRAF6 possesses ubiquitin ligase activity that controls the activation of IKK and NF-kappaB. Because these studies are primarily based on cell-free systems, the role of the ubiquitin ligase activity of TRAF6 and its auto-ubiquitination to initiate the NF-kappaB pathway in vivo remain elusive. Here we show that an intact RING domain of TRAF6 in conjunction with the E2 enzym"],"journal":["The Journal of biological chemistry"],"pubmed_title":["Site-specific Lys-63-linked tumor necrosis factor receptor-associated factor 6 auto-ubiquitination is a critical determinant of I kappa B kinase activation."],"pmcid":["PMC3221607"],"funding_grant_id":["R01 AR053540-04","P30 CA016672","R01 AI045937","R01 AR053540","CA16672DAF","R01-AI 45937"],"pubmed_authors":["Webster WK","Lamothe B","Besse A","Campos AD","Darnay BG","Wu H"],"additional_accession":[]},"is_claimable":false,"name":"Site-specific Lys-63-linked tumor necrosis factor receptor-associated factor 6 auto-ubiquitination is a critical determinant of I kappa B kinase activation.","description":"Tumor necrosis factor (TNF) receptor-associated factor 6 (TRAF6) is a key mediator in proximal signaling of the interleukin-1/Toll-like receptor and the TNF receptor superfamily. Analysis of TRAF6-deficient mice revealed a fundamental role of TRAF6 in osteoclastogenesis; however, the molecular mechanism underlying TRAF6 signaling in this biological process is not understood. Recent biochemical evidence has indicated that TRAF6 possesses ubiquitin ligase activity that controls the activation of IKK and NF-kappaB. Because these studies are primarily based on cell-free systems, the role of the ubiquitin ligase activity of TRAF6 and its auto-ubiquitination to initiate the NF-kappaB pathway in vivo remain elusive. Here we show that an intact RING domain of TRAF6 in conjunction with the E2 enzym","dates":{"release":"2007-01-01T00:00:00Z","publication":"2007 Feb","modification":"2025-04-05T13:52:11.229Z","creation":"2019-03-27T00:46:14Z"},"accession":"S-EPMC3221607","cross_references":{"pubmed":["17135271"],"doi":["10.1074/jbc.M609503200","10.1074/jbc.m609503200"]}}