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The Cdc37 protein kinase-binding domain is sufficient for protein kinase activity and cell viability.

http://www.ncbi.nlm.nih.gov/pubmed/12499358

Cdc37 is a molecular chaperone required for folding of protein kinases. It functions in association with Hsp90, although little is known of its mechanism of action or where it fits into a folding pathway involving other Hsp90 cochaperones. Using a genetic approach with Saccharomyces cerevisiae, we show that CDC37 overexpression suppressed a defect in v-Src folding in yeast deleted for STI1, which recruits Hsp90 to misfolded clients. Expression of CDC37 truncation mutants that were deleted for the Hsp90-binding site stabilized v-Src and led to some folding in both sti1Delta and hsc82Delta strains. The protein kinase-binding domain of Cdc37 was sufficient for yeast cell viability and permitted efficient signaling through the yeast MAP kinase-signaling pathway. We propose a model in which Cdc37 can function independently of Hsp90, although its ability to do so is restricted by its normally low expression levels. This may be a form of regulation by which cells restrict access to Cdc37 until it has passed through a triage involving other chaperones such as Hsp70 and Hsp90.

Pubmed ID: 12499358 RIS Download

Mesh terms: Binding Sites | Blotting, Western | Cell Cycle Proteins | Drosophila Proteins | Genetic Complementation Test | Glutathione Transferase | HSP70 Heat-Shock Proteins | HSP90 Heat-Shock Proteins | MAP Kinase Signaling System | Models, Biological | Molecular Chaperones | Mutation | Oncogene Protein pp60(v-src) | Plasmids | Protein Binding | Protein Folding | Protein Structure, Tertiary | Protein-Tyrosine Kinases | Saccharomyces cerevisiae | Saccharomyces cerevisiae Proteins | Signal Transduction | Temperature