Journal
PROTEOMICS
Volume 10, Issue 12, Pages 2337-2347Publisher
WILEY
DOI: 10.1002/pmic.201000130
Keywords
Actin; Cell biology; HSPA8; Interacting proteins; MIP-T3
Funding
- Japan Society for the Promotion of Science
- State Key Laboratory of Virology of China [2009003]
- 2007 Chang-Jiang Scholars Program
- 211 Projects
- Talents Start-up Foundation of Jinan University [51207040]
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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.
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