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A novel family of putative signal transducers associated with the cytoplasmic domain of the 75 kDa tumor necrosis factor receptor.

Mutational analysis identified a C-terminal region of 78 amino acids within the cytoplasmic domain of the human 75 kDa tumor necrosis factor receptor (TNF-R2) that is required for signal transduction. This region was subsequently shown to mediate the interaction of cytoplasmic factors with TNF-R2. Two of these factors were isolated and molecularly cloned using biochemical purification and the yeast two-hybrid system. TNF receptor-associated factor 1 (TRAF1) and TRAF2 are the first two members of a novel protein family containing a novel C-terminal homology region, the TRAF domain. In addition, TRAF2 contains an N-terminal RING finger motif. TRAF1 and TRAF2 can form homo- and heterotypic dimers. Our analysis indicates that TRAF1 and TRAF2 are associated with the cytoplasmic domain of TNF-R2 in a heterodimeric complex in which TRAF2 contacts the receptor directly. TRAF1 interacts with TNF-R2 indirectly through heterodimer formation with TRAF2.

Pubmed ID: 8069916

Authors

  • Rothe M
  • Wong SC
  • Henzel WJ
  • Goeddel DV

Journal

Cell

Publication Data

August 26, 1994

Associated Grants

None

Mesh Terms

  • Amino Acid Sequence
  • Animals
  • Antigens, CD
  • Base Sequence
  • Cloning, Molecular
  • Cytoplasm
  • Humans
  • Mice
  • Models, Biological
  • Molecular Sequence Data
  • Organ Specificity
  • Protein Conformation
  • Protein Structure, Tertiary
  • Proteins
  • RNA, Messenger
  • Receptors, Tumor Necrosis Factor
  • Receptors, Tumor Necrosis Factor, Type II
  • Recombinant Fusion Proteins
  • Sequence Alignment
  • Sequence Analysis
  • Sequence Analysis, DNA
  • Sequence Homology, Amino Acid
  • Signal Transduction
  • TNF Receptor-Associated Factor 1
  • TNF Receptor-Associated Factor 2