Proteomic analysis reveals novel binding partners of MIP-T3 in human cells
Proteomic analysis reveals novel binding partners of MIP-T3 in human cells
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DOI：
10.1002/pmic.201000130
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发表时间：
2010-06-01
期刊：
影响因子：
3.4
通讯作者：
Kitazato, Kaio
中科院分区：
文献类型：
--
作者：
Guo, Chao-Wan;Xiong, Sheng;Kitazato, Kaio
MIP-T3（microtubule-interacting protein associated with TRAF 3）是一种微管相互作用蛋白，从蠕虫到人类在进化上保守，但其细胞功能仍然未知。为了深入了解MIP-T3的功能，我们开始在人胚肾293细胞中通过免疫沉淀和MS分析来鉴定MIP-T3相互作用蛋白。结果，共鉴定出34个蛋白质，其中大部分是新的MIP-T3推定伴侣。根据MIP-T3相关蛋白的分子功能可将其分为9类，包括细胞骨架、分子伴侣、核酸结合、激酶等，并通过免疫共沉淀和共定位分析进一步确定了3种MIP-T3相互作用蛋白-- actin、HSPA 8和tubulin。MIP-T3与肌动蛋白丝和微管的相互作用表明，MIP-T3可能在调节细胞骨架动力学中起重要作用。因此，我们的研究结果不仅揭示了大量具有多种细胞功能的MIP-T3相关蛋白，而且为MIP-T3功能的研究提供了新的研究方向。
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.