Structural Studies of Human TRAF2

  1. H. WU,
  2. Y.C. PARK,
  3. H. YE, and
  4. L. TONG
  1. *Department of Biochemistry, The Weill Medical College of Cornell University, New York, New York 10021;Department of Biological Sciences, Columbia University, New York, New York 10027

This extract was created in the absence of an abstract.

Excerpt

The tumor necrosis factor (TNF) receptor (TNFR) superfamily effects a wide spectrum of cellular responses including proliferation, differentiation, and apoptosis (for review,see Smith et al. 1994). Current members of TNFRs includeTNF-R1, TNF-R2, Fas, CD40, CD30, CD27, LTβR, Ox40,4-1BB, RANK, p75 nerve growth factor (NGF) receptor,and a series of death receptors (DRs). Recent studies haveimplicated the TNFR-associated factors (TRAFs) as majorsignal transducers for many members of this receptor superfamily (for review, see Arch et al. 1998). The Epstein-Barr virus (EBV) oncogene product LMP1 also usesTRAFs for inducing long-term growth potentiation and celltransformation (Mosialos et al. 1995). In addition, TRAFsignaling is important for receptors of the pro-inflammatorycytokine interleukin-1 (IL-1) (Cao et al. 1996b). The downstream signaling of TRAFs appears to involve the activation of kinases in the MAPK family, leading eventually tothe activation of Rel (NF-κB) and AP-1 transcription factors (for review, see Arch et al. 1998). These transcriptionfactors can switch on various genes involved in inflammatory, immune, and acute phase responses...

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