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Updated: Jul 14, 2026

Peptide-based Identification of Functional Motifs and their Binding Partners
14:28

Peptide-based Identification of Functional Motifs and their Binding Partners

Published on: June 30, 2013

Physical and functional interaction between mortalin and Mps1 kinase

Masayuki Kanai1, Zhiyong Ma, Hideki Izumi

  • 1Department of Cell Biology, University of Cincinnati College of Medicine, Cincinnati, OH 45267, USA.

Genes to Cells : Devoted to Molecular & Cellular Mechanisms
|June 19, 2007
PubMed

Insights

Mortalin (Hsp70 chaperone) interacts with Mps1 kinase, leading to mortalin phosphorylation and Mps1 super-activation. This interaction is crucial for mortalin

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Protein Interactions

Background:

  • Mortalin, a member of the Hsp70 chaperone family, participates in diverse cellular processes.
  • Mps1 kinase is known to regulate centrosome duplication and the mitotic checkpoint.
  • Mortalin's role in centrosome duplication and its centrosomal localization have been previously suggested.

Purpose of the Study:

  • To identify kinases that physically interact with mortalin.
  • To elucidate the functional consequences of the mortalin-Mps1 interaction.
  • To investigate the role of Mps1 in mortalin's centrosomal localization and function.

Main Methods:

  • Identification of mortalin-interacting kinases.
  • Analysis of mortalin phosphorylation by Mps1 at specific residues (Thr62 and Ser65).
  • Assessment of Mps1 activity modulation by phosphorylated mortalin.
  • Investigation of mortalin's centrosomal localization in the presence and absence of Mps1.
  • Evaluation of Mps1-driven centrosome duplication acceleration with and without mortalin.

Main Results:

  • Mps1 was identified as a kinase that physically interacts with mortalin.
  • Mps1 phosphorylates mortalin on Thr62 and Ser65, which in turn super-activates Mps1.
  • Centrosomal localization of mortalin is dependent on the presence of Mps1.
  • Mps1-accelerated centrosome duplication requires both mortalin and its Mps1-mediated phosphorylation.

Conclusions:

  • Mortalin and Mps1 form a regulatory feedback loop where Mps1 phosphorylates mortalin, leading to Mps1 super-activation.
  • Mps1 is essential for the centrosomal localization of mortalin.
  • The mortalin-Mps1 interaction, including mortalin phosphorylation, plays a critical role in regulating centrosome duplication.

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