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Physical and functional interaction between mortalin and Mps1 kinase
Author(s) -
Kanai Masayuki,
Ma Zhiyong,
Izumi Hideki,
Kim SongHee,
Mattison Christopher P.,
Winey Mark,
Fukasawa Kenji
Publication year - 2007
Publication title -
genes to cells
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.912
H-Index - 115
eISSN - 1365-2443
pISSN - 1356-9597
DOI - 10.1111/j.1365-2443.2007.01091.x
Subject(s) - centrosome , biology , kinase , microbiology and biotechnology , mitosis , gene duplication , phosphorylation , gene , cell cycle , genetics
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.