Physical and functional interaction between mortalin and Mps1 kinase

被引:43
作者
Kanai, Masayuki
Ma, Zhiyong
Izumi, Hideki
Kim, Song-Hee
Mattison, Christopher P.
Winey, Mark
Fukasawa, Kenji [1 ]
机构
[1] Univ Cincinnati, Coll Med, Dept Cell Biol, Cincinnati, OH 45267 USA
[2] Shanghai Vet Res Inst, Dept Anim Infect Dis, Shanghai 200232, Peoples R China
[3] Univ Colorado, Dept Mol Cellular & Dev Biol, Boulder, CO 80309 USA
关键词
D O I
10.1111/j.1365-2443.2007.01091.x
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Mortalin is a member of Hsp70 chaperoning protein family involved in various cellular functions. Through the search of the kinases that mortalin physically interact with, we identified Mps1 as such a kinase. Mps1 kinase has been implicated in the regulation of centrosome duplication and mitotic checkpoint response. Mortalin binds to Mps1, and is phosphorylated by Mps1 on Thr62 and Ser65. The phosphorylated mortalin then super-activates Mps1 in a feedback manner. Mortalin has been previously shown to localize to centrosomes, and to be involved in the regulation of centrosome duplication. We found that centrosomal localization of mortalin depends on the presence of Mps1. Moreover, Mps1-associated acceleration of centrosome duplication depends on the presence of mortalin and super-activation by the Thr62/Ser65 phosphorylated mortalin.
引用
收藏
页码:797 / 810
页数:14
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