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

Proteomics. 2010 Jun;10(12):2337-47. doi: 10.1002/pmic.201000130.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actins / metabolism
  • Blotting, Western
  • Carrier Proteins / metabolism*
  • Cell Line
  • Cell Line, Tumor
  • Humans
  • Immunoprecipitation
  • Microscopy, Confocal
  • Microtubule-Associated Proteins / metabolism*
  • Microtubules / metabolism
  • Protein Binding
  • Proteomics*

Substances

  • Actins
  • Carrier Proteins
  • Microtubule-Associated Proteins
  • TRAF3IP1 protein, human