Physical and functional interaction between mortalin and Mps1 kinase

Masayuki Kanai, Zhiyong Ma, Hideki Izumi, Song Hee Kim, Christopher P. Mattison, Mark Winey, Kenji Fukasawa

Research output: Contribution to journalArticle

44 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)797-810
Number of pages14
JournalGenes to Cells
Volume12
Issue number6
DOIs
StatePublished - Jun 1 2007
Externally publishedYes

ASJC Scopus subject areas

  • Genetics
  • Cell Biology

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    Kanai, M., Ma, Z., Izumi, H., Kim, S. H., Mattison, C. P., Winey, M., & Fukasawa, K. (2007). Physical and functional interaction between mortalin and Mps1 kinase. Genes to Cells, 12(6), 797-810. https://doi.org/10.1111/j.1365-2443.2007.01091.x