PubMed:20184394 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PubMed/sourceid/20184394","sourcedb":"PubMed","sourceid":"20184394","source_url":"http://www.ncbi.nlm.nih.gov/pubmed/20184394","text":"TACI induces cIAP1-mediated ubiquitination of NIK by TRAF2 and TANK to limit non-canonical NF-kappaB signaling.\nB-cell-activating factor of the TNF family (BAFF) is a critical factor for B-cell survival and maturation through non-canonical nuclear factor kappaB (NF-kappaB) pathway, a NF-kappaB inducing kinase (NIK)-dependent pathway for the processing of NF-kappaB2 p100 to generate p52. While BAFF acts primarily through BAFF receptor (BAFF-R), the transmembrane activator and CAML interactor (TACI), the other receptor for BAFF, is thought to serve as a negative regulator for B-cell responses. However, how TACI regulates NF-kappaB2 activity is largely unknown. In this study, we showed that constitutive activation of TACI signaling suppressed BAFF-R-mediated NF-kappaB2 p100 processing with the up-regulation of cellular inhibitors of apoptosis 1 (cIAP1) and TNF receptor associated factor (TRAF)-associated NF-kappaB activator (TANK). The ubiquitination of NIK by cIAP1 was inhibited by the expression of TRAF2 with physical binding to cIAP1. TANK deficiency by small interfering RNA (siRNA) impaired TACI-dependent inhibition of NF-kappaB2 p100 processing. TANK also inhibited TRAF2-mediated cIAP1 inactivation. Moreover, the recruitment of TRAF2 to TACI induced the ubiquitination of NIK. Taken together, the regulation of NIK by TACI through the interaction of TANK/TRAF2/cIAP1 plays a pivotal role in the suppression of non-canonical NF-kappaB 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