TRAF1 and Its Biological Functions
Tumor necrosis factor (TNF) receptor-associated factor (TRAF)1 was originally identified based on its ability to interact with the cytosolic domain of TNF receptor type 2 (TNFR2). TRAF1 is unique among TRAF proteins in that it lacks RING domain found in the N-terminal regions of other TRAFs. TRAF1 can associate with multiple TNFR family members and can also bind several protein kinases and adaptor proteins suggesting that this protein likely possesses multiple functions in cytokine signaling networks. Although our understanding of TRAF1 functions and the underlying mechanisms at molecular and cellular levels has been advanced in recent years, much still needs to be learned before we have a full grasp of TRAF1 biology.
KeywordsTumor Necrosis Factor Receptor Tumor Necrosis Factor Receptor Superfamily Tumor Necrosis Factor Signaling Tumor Necrosis Factor Ligand Tumor Necrosis Factor Receptor Type
Unable to display preview. Download preview PDF.
- 3.Kaufman D, Choi Y. Signaling by tumor necrosis factor receptors: Pathways, paradigms and targets for therapeutic modulation. Intern Rev Immunol 1999; 18:405–427.Google Scholar
- 19.Schwenzer R, Siemienski K, Liptay S et al. The human tumor necrosis factor (TNF) receptor-associated factor 1 gene (TRAF1) is up-regulated by cytokines of the TNF ligand family and modulates TNF-induced activation of NF-κB and c-Jun N-terminal kinase. J Biol Chem 1999; 274:19368–19374.PubMedCrossRefGoogle Scholar
- 23.Zapata JM, Reed JC. TRAF1: Lord without a RING. Sci STKE 2002; 21:PE27.Google Scholar
- 42.Henkler F, Baumann B, Fotin-Mleczek M et al. Caspase-mediated cleavage converts the tumor necrosis factor (TNF) receptor-associated factor (TRAF)-1 from a selective modulator of TNF receptor signaling to a general inhibitor of NF-κB activation. J Biol Chem 2003; 278:29216–29230.PubMedCrossRefGoogle Scholar