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A role for Hsp90 in cell cycle control: Wee1 tyrosine kinase activity requires interaction with Hsp90

R Aligue1, H Akhavan-Niak, P Russell

  • 1Department of Molecular Biology, Scripps Research Institute, La Jolla, CA 92037.

The EMBO Journal
|December 15, 1994
PubMed

Insights

The Hsp90 chaperone protein Swo1 is essential for the activity of Wee1 kinase, which controls cell cycle progression. This discovery reveals a novel role for Hsp90 in regulating the cell cycle.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Wee1 protein kinase regulates the G2 phase length via inhibitory phosphorylation of Cdc2-cyclin B.
  • Cell cycle arrest can be caused by the overproduction of Wee1 kinase.

Purpose of the Study:

  • To investigate the genetic interactions between Wee1 and suppressors of Wee1 overproduction.
  • To elucidate the molecular function of the suppressor of wee1 overproduction 1 (swo1) gene.

Main Methods:

  • Isolation and characterization of suppressor of wee1 overproduction (swo) mutations.
  • Genetic analysis in a wee1+ background.
  • Coimmunoprecipitation assays to detect protein interactions.
  • Phenotypic analysis of mutant strains at different temperatures.

Main Results:

  • A class of mutations, swo1, suppressed Wee1 overproduction-induced G2 arrest and caused temperature-sensitive lethality.
  • The swo1+ gene encodes a member of the Hsp90 family of chaperone proteins.
  • Swo1 coimmunoprecipitated with Wee1, indicating a physical interaction.
  • The swo1-26 mutant exhibited premature mitosis at semi-permissive temperatures.

Conclusions:

  • The Hsp90 chaperone Swo1 is required for the formation of active Wee1 tyrosine kinase.
  • This interaction is crucial for proper cell cycle control, specifically regulating the G2/M transition.
  • Hsp90 plays an unexpected but vital role in cell cycle regulation through its interaction with Wee1.

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