Cdc37 regulation of the kinome: when to hold 'em and when to fold 'em

Sci STKE. 2007 May 8;2007(385):pe22. doi: 10.1126/stke.3852007pe22.

Abstract

Although massive genome sequencing efforts have identified the protein kinases encoded by several eukaryotic genomes and proteomic analyses have begun to determine the kinases expressed in a cell, there is still much to learn about the additional cellular events that shape eukaryotic kinomes. Large-scale analyses in Saccharomyces cerevisiae have indicated that a relatively small subset of kinases requires chaperoning by heat shock protein 90 (Hsp90). However, new evidence suggests that most kinases do require chaperoning and, furthermore, that Cdc37, a chaperone that has Hsp90-dependent and -independent functions, serves as the chaperone for a large portion of the yeast kinome.

Publication types

  • Review

MeSH terms

  • Cell Cycle Proteins / genetics
  • Cell Cycle Proteins / metabolism*
  • Genome, Fungal / physiology*
  • HSP90 Heat-Shock Proteins / genetics
  • HSP90 Heat-Shock Proteins / metabolism*
  • Molecular Chaperones / genetics
  • Molecular Chaperones / metabolism*
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae / metabolism*
  • Saccharomyces cerevisiae Proteins / genetics
  • Saccharomyces cerevisiae Proteins / metabolism*

Substances

  • CDC37 protein, S cerevisiae
  • Cell Cycle Proteins
  • HSP82 protein, S cerevisiae
  • HSP90 Heat-Shock Proteins
  • Molecular Chaperones
  • Saccharomyces cerevisiae Proteins