Journal
JOURNAL OF CELL BIOLOGY
Volume 159, Issue 6, Pages 1051-1059Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.200210121
Keywords
chaperone; Cdc37; v-Src; Hsp90; yeast
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Funding
- NIDDK NIH HHS [T32 DK007645, 5T32DK07645, DK60598, R01 DK060598] Funding Source: Medline
- NIGMS NIH HHS [GM66644, F32 GM066644] Funding Source: Medline
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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.
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