MIP-T3, a Novel Protein Linking Tumor Necrosis Factor Receptor-associated Factor 3 to the Microtubule Network
Copyright policy )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.
Binding Sites, Membrane Glycoproteins, Paclitaxel, CD40 Ligand, Molecular Sequence Data, Proteins, Receptors, Cell Surface, Microtubules, Receptors, Tumor Necrosis Factor, Protein Structure, Tertiary, Mutation, Humans, Amino Acid Sequence, CD40 Antigens, Microtubule-Associated Proteins, Cytoskeleton, Gene Library, HeLa Cells, Protein Binding, Sequence Deletion
Binding Sites, Membrane Glycoproteins, Paclitaxel, CD40 Ligand, Molecular Sequence Data, Proteins, Receptors, Cell Surface, Microtubules, Receptors, Tumor Necrosis Factor, Protein Structure, Tertiary, Mutation, Humans, Amino Acid Sequence, CD40 Antigens, Microtubule-Associated Proteins, Cytoskeleton, Gene Library, HeLa Cells, Protein Binding, Sequence Deletion
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