TNF receptor-associated factor (TRAF) 3 is an intracellular protein that belongs to the TRAF family of molecules. The characteristic feature of TRAFs is a domain structure that includes (except TRAF1) Zn-binding RING and Finger domains, coiled-coil domains (TRAF-N) that promote multimer formation, and (except TRAF7) a TRAF-C domain important for interaction with cellular receptors and regulation of signaling pathways (Xie 2013). TRAF3 has many cell type- and context-specific roles, primarily as an adaptor protein with a large variety of binding partners.
Early attempts to characterize TRAF3 in vivo functions were hindered by the lack of useful animal models, as global deletion of TRAF3 in mice leads to hypoglycemia, leukopenia, and early postnatal lethality (Xu et al. 1996). Alternative models to study TRAF molecules relied on exogenous overexpression in epithelial and fibroblast cell lines, with NF-κB activation as the...
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