TRAF4 (D1N3A) Rabbit mAb #18527

TRAFs (TNF receptor-associated factors) are a family of multifunctional adaptor proteins that bind to surface receptors and recruit additional proteins to form multiprotein signaling complexes capable of promoting cellular responses (1-3). Members of the TRAF family share a common carboxy-terminal "TRAF domain", which mediates interactions with associated proteins; many also contain amino-terminal Zinc/RING finger motifs. The first TRAFs identified, TRAF1 and TRAF2, were found by virtue of their interactions with the cytoplasmic domain of TNF-receptor 2 (TNFRII) (4). The six known TRAFs (TRAF1-6) act as adaptor proteins for a wide range of cell surface receptors and participate in the regulation of cell survival, proliferation, differentiation, and stress responses.
TRAF4, also referred to as CART1 and MLN62, is a divergent member of the TRAF family with relatively weak binding to TNFR family members (5-7). Interactions have been observed between TRAF4 and the neurotrophin receptor p75-NGFR, lymphotoxin-β receptor, and GITR (8-10). While originally identified in metastatic breast carcinoma, TRAF4 has been shown to contribute to tumor growth and invasion in various cancers including breast, lung and colon (11-13). Expression of Traf4 is induced by the tumor suppressor p53 in response to DNA damage, and can promote apoptosis (14).TRAF4 has also been shown to play a critical role in TGF-β signaling, where it has been found to antagonize the E3 ligase Smurf, resulting in enhanced receptor stabilization driving breast cancer metastasis (15).