Proteomic analysis reveals novel binding partners of MIP-T3 in human cells.

Division of Molecular Pharmacology of Infectious agents, Department of Molecular Microbiology and Immunology, Graduate School of Biomedical Sciences, Nagasaki University, Nagasaki City, Nagasaki, Japan.
MIP-T3 (microtubule-interacting protein associated with TRAF3) is a microtubule-interacting protein that evolutionarily conserved from worms to humans, but whose cellular functions remains unknown. To get insight into the functions of MIP-T3, we set out to identify MIP-T3 interacting proteins by immunoprecipitation in human embryonic kidney 293 cells and MS analysis. As the results, a total of 34 proteins were identified and most of them were novel MIP-T3 putative partners. The MIP-T3-associated proteins could be grouped into nine clusters based on their molecule functions, including cytoskeleton, chaperone, nucleic acid binding, kinase and so on. Three MIP-T3-interacted proteins - actin, HSPA8 and tubulin - were further confirmed by reciprocal coimmunoprecipitations and colocalization analysis. The interaction of MIP-T3 with both actin filaments and microtubule suggested that MIP-T3 may play an important role in regulation of cytoskeleton dynamics in cells. Our results therefore not only uncover a large number of MIP-T3-associated proteins that possess a variety of cellular functions, but also provide new research directions for the study of the functions of MIP-T3.
Mesh Terms:
Actins, Blotting, Western, Carrier Proteins, Cell Line, Cell Line, Tumor, Humans, Immunoprecipitation, Microscopy, Confocal, Microtubule-Associated Proteins, Microtubules, Protein Binding, Proteomics
Proteomics Jun. 01, 2010; 10(12);2337-47 [PUBMED:20391533]
Download 42 Interactions For This Publication
Switch View:
  • Interactions (42)