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 RIS Download
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