Nonredundant and complementary functions of TRAF2 and TRAF3 in a ubiquitination cascade that activates NIK-dependent alternative NF-κB signaling

By Sivakumar Vallabhapurapu, A. Matsuzawa, Weizhou Zhang, Ping-Hui Tseng, J. Keats, Haopeng Wang, D. Vignali, P. Bergsagel, M. Karin. Nature Immunology, 2008

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The Regulation of NF-κB Subunits by Phosphorylation (2016, background): “Once bound to p100 NIK phosphorylates and activates IKKα [38,39].”
Molecular mechanism and function of CD40/CD40L engagement in the immune system (2009, background): “cIAP1 ⁄ 2 degrades NIK, ablating the non-canonical NFjB pathway (39, 40).”
Cracking the BAFF code (2009, background): “In the presence of BAFF, TRAF3 is recruited to BAFFR and degraded in a TRAF2-dependent manner, resulting in the stabilization of NIK and activation of NF-κB2, which then leads to increased B cell surviva”
The noncanonical NF‐κB pathway (2012, background): “cells, TRAF2 is required for signal-induced degradation of TRAF3 (30, 65), thus contributing to inducible NIK stabilization.”
Is NF-κB a good target for cancer therapy? Hopes and pitfalls (2009, background): “Recent work indicates that NIK degradation in resting cells depends on its association with TRAF3, which serves as an adaptor that recruits NIK to a ubiquitin ligase complex composed of TRAF2 and cIAP1/2 (Ref”