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

      1 , , ,
      Cell
      Elsevier BV

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          Abstract

          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.

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          Author and article information

          Journal
          Cell
          Cell
          Elsevier BV
          0092-8674
          0092-8674
          Aug 26 1994
          : 78
          : 4
          Affiliations
          [1 ] Department of Molecular Biology, Genentech, Incorporated, South San Francisco, California 94080.
          Article
          0092-8674(94)90532-0
          10.1016/0092-8674(94)90532-0
          8069916
          a1a2b4d2-eb12-4c7f-b38d-47d72e015d50
          History

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