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Published online January 22, 2007
doi:10.1083/jcb.200604106
The Journal of Cell Biology, Vol. 176, No. 3, 319-328
The Rockefeller University Press, 0021-9525 $30.00
© 2007 Mandal et al.
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Article

 Cdc37 has distinct roles in protein kinase quality control that protect nascent chains from degradation and promote posttranslational maturation

Atin K. Mandal1, Paul Lee1, Jennifer A. Chen1, Nadinath Nillegoda1, Alana Heller1, Susan DiStasio1, Handy Oen1, Jacob Victor1, Devi M. Nair1, Jeffrey L. Brodsky2, and Avrom J. Caplan1

1 Department of Pharmacology and Biological Chemistry, Mount Sinai School of Medicine, New York, NY 10029
2 Department of Biological Sciences, University of Pittsburgh, Pittsburgh, PA 15260

Correspondence to Avrom J. Caplan: avrom.caplan{at}mssm.edu

Cdc37 is a molecular chaperone that functions with Hsp90 to promote protein kinase folding. Analysis of 65 Saccharomyces cerevisiae protein kinases (~50% of the kinome) in a cdc37 mutant strain showed that 51 had decreased abundance compared with levels in the wild-type strain. Several lipid kinases also accumulated in reduced amounts in the cdc37 mutant strain. Results from our pulse-labeling studies showed that Cdc37 protects nascent kinase chains from rapid degradation shortly after synthesis. This degradation phenotype was suppressed when cdc37 mutant cells were grown at reduced temperatures, although this did not lead to a full restoration of kinase activity. We propose that Cdc37 functions at distinct steps in kinase biogenesis that involves protecting nascent chains from rapid degradation followed by its folding function in association with Hsp90. Our studies demonstrate that Cdc37 has a general role in kinome biogenesis.

Abbreviations used in this paper: MBP, myelin basic protein; TAP, tandem affinity purified.


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