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Tumor necrosis factor (TNF) receptor associated factors (TRAFs) were initially discovered as adaptor proteins that link the TNF receptor superfamily to signaling pathways and are thus important regulators of cell death and cellular response to stress.1 TRAF proteins share a homology region that allows them to bind to cell receptors and other TRAF proteins, causing the activation of different signal cascades depending on the TRAFs involved. For example, TRAF2 and TRAF3 directly bind to the CD40, a NF receptor superfamily member involved in inducing B cell immunity,2 and are critical for NF-κB activation in mouse B lymphocytes.3 TRAF2 along with TRAF6 has also been shown to be required for CD40 signaling in nonhemopoietic cells.4 TRAF2 also interacts with the TRFR superfamily member lymphotoxin-b receptor (LTbR) in association with TRAF3 and the apoptosis inhibitors cIAP1 and Smac.