MIP-T3, a novel protein linking tumor necrosis factor receptor-associated factor 3 to the microtubule network.

In this study, we report the identification of a novel tumor necrosis factor receptor-associated factor 3 (TRAF3)-interacting protein designated MIP-T3. MIP-T3 is a 83-kDa protein with no significant homology to known mammalian proteins. MIP-T3 mRNA and TRAF3 mRNA are ubiquitously expressed, and TRAF3 is the only TRAF protein to interact ...
with MIP-T3. The MIP-T3-TRAF3 interaction requires the coiled-coil TRAF-N domain of TRAF3. To our knowledge, this is the first case of a TRAF-binding protein that interacts with a single member of the TRAF family specifically through a TRAF-N coiled-coil domain. MIP-T3 binds to Taxol-stabilized microtubules and to tubulin in vitro, and MIP-T3 recruits TRAF3 to microtubules when both proteins are overexpressed in HeLa cells. In a 293 cell line stably expressing CD40, TRAF3 is released from the TRAF3.MIP-T3 complex and recruited to the CD40 receptor upon CD40 ligand stimulation. MIP-T3 may provide a novel mechanism in sequestering TRAF3 to the cytoskeletal network.
Mesh Terms:
Amino Acid Sequence, Antigens, CD40, Binding Sites, CD40 Ligand, Cytoskeleton, Gene Library, Hela Cells, Humans, Membrane Glycoproteins, Microtubule-Associated Proteins, Microtubules, Molecular Sequence Data, Mutation, Paclitaxel, Protein Binding, Protein Structure, Tertiary, Proteins, Receptors, Cell Surface, Receptors, Tumor Necrosis Factor, Sequence Deletion, TNF Receptor-Associated Factor 3, Two-Hybrid System Techniques
J. Biol. Chem.
Date: Aug. 04, 2000
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