A novel member of the TRAF family of putative signal transducing proteins binds to the cytosolic domain of CD40.

CD40 is a member of the tumor necrosis factor receptor (TNF-R) family that regulates B-lymphocyte proliferation, immunoglobulin class-switching, and apoptosis through poorly defined signal transduction mechanisms. Using a yeast two-hybrid method, cDNAs were obtained that encode a novel protein, CD40-associated protein-1 (CAP-1), which binds specifically to the cytosolic domain of ...
CD40 but not TNF-R1, TNF-R2, or Fas. The CAP-1 protein contains a C-terminal domain that shares strong amino acid sequence homology with a unique domain found recently in two putative signal transducing proteins that bind to the TNF-R2 cytosolic tail, TRAF1 and TRAF2. This C-terminal region of CAP-1 was sufficient to mediate binding to CD40 and homodimerization of CAP-1 proteins. The N-terminal portion of CAP-1 contains a RING finger motif and three zinc finger-like domains similar to those found in several regulatory proteins that interact with DNA or RNA. CAP-1 thus represents a new member of a family of potential signal transducing proteins that contain a conserved domain (the TRAF domain), bind to the cytosolic regions of particular members of TNF-R family proteins, and that can form homo- and heterotypic dimers.
Mesh Terms:
Amino Acid Sequence, Antigens, CD, Antigens, CD40, Antigens, Differentiation, B-Lymphocyte, Base Sequence, Carrier Proteins, Cells, Cultured, Cloning, Molecular, Cytosol, DNA, Complementary, Humans, Molecular Sequence Data, Open Reading Frames, Protein Binding, Sequence Homology, Amino Acid, Signal Transduction, TNF Receptor-Associated Factor 3, Tumor Necrosis Factor Receptor-Associated Peptides and Proteins
FEBS Lett.
Date: Jan. 23, 1995
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