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.
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
Cell
Date: Aug. 26, 1994
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