TRAF1 and its biological functions

Adv Exp Med Biol. 2007;597:25-31. doi: 10.1007/978-0-387-70630-6_2.

Abstract

Tumor necrosis factor (TNF) receptor-associated factor (TRAF)1 was originally identified based on its ability to interact with the cytosolic domain ofTNF 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 ofTRAF 1 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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Humans
  • TNF Receptor-Associated Factor 1 / biosynthesis
  • TNF Receptor-Associated Factor 1 / chemistry
  • TNF Receptor-Associated Factor 1 / genetics
  • TNF Receptor-Associated Factor 1 / physiology*

Substances

  • TNF Receptor-Associated Factor 1