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The molecular chaperone Cdc37 is required for Ste11 function and pheromone-induced cell cycle arrest.

The molecular chaperone Cdc37 is thought to act in part as a targeting subunit of the heat-shock protein 90 (Hsp90) chaperone complex. We demonstrate here that Cdc37 is required for activity of the kinase Ste11 in budding yeast. A cdc37 mutant strain is defective in Ste11-mediated pheromone signaling and in accumulation and functional maturation of the constitutively active Ste11 version Ste11DeltaN. Moreover, Cdc37, Ste11DeltaN and Hsp90 coprecipitate pairwise. Thus, Hsp90 and Cdc37 may transiently associate with Ste11 to promote proper folding and/or association with additional regulatory factors. Our results establish Ste11 as the first endogenous Cdc37 client protein in yeast.

Pubmed ID: 10664467


  • Abbas-Terki T
  • DonzĂ© O
  • Picard D


FEBS letters

Publication Data

February 4, 2000

Associated Grants


Mesh Terms

  • Alleles
  • Cell Cycle
  • Cell Cycle Proteins
  • Drosophila Proteins
  • Enzyme Activation
  • Fungal Proteins
  • HSP90 Heat-Shock Proteins
  • MAP Kinase Kinase Kinases
  • MAP Kinase Signaling System
  • Molecular Chaperones
  • Mutation
  • Pheromones
  • Phosphorylation
  • Protein Binding
  • Protein Isoforms
  • Recombinant Fusion Proteins
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Schizosaccharomyces pombe Proteins
  • Temperature
  • Transcription Factors