Tumor necrosis factor receptor (TNFR) superfamily members transmit signals regulating proliferation, differentiation and apoptosis in various types of cells. TNFR-associated factors (TRAFs) are a family of proteins that were initially discovered as downstream signal transducers of the TNFR superfamily. TRAF3 contains an N-terminal ring finger/zinc finger region that is thought to be essential for downstream signaling. MIP-T3 is associated with TRAF3. MIP-T3 binds to taxol-stabilized microtubules and to tubulin in vitro, and MIP-T3 recruits TRAF3 to microtubules when both proteins are overexpressed. The MIP-T3/TRAF3 interaction requires the coiled-coil TRAF-N domain of TRAF3. This interaction may provide a novel mechanism in sequestering TRAF3 to the cytoskeletal network.
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Protein Aliases: interleukin 13 receptor alpha 1-binding protein-1; Interleukin-13 receptor alpha 1-binding protein 1; Intraflagellar transport protein 54 homolog; microtubule interacting protein that associates with TRAF3; Microtubule-interacting protein associated with TRAF3; microtubule-interacting protein that associates with TRAF3; MIP-T3; TNF receptor-associated factor 3 interacting protein 1; TRAF3-interacting protein 1
Gene Aliases: 3930402D05Rik; AU041749; IFT54; MIP-T3; MIPT3; SLSN9; TRAF3IP1