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Sci. STKE, 8 May 2007
Vol. 2007, Issue 385, p. pe22
[DOI: 10.1126/stke.3852007pe22]

PERSPECTIVES

Cdc37 Regulation of the Kinome: When to Hold ‘Em and When to Fold ‘Em

Larry M. Karnitz1* and Sara J. Felts2

1Department of Molecular Pharmacology and Experimental Therapeutics and
2Department of Biochemistry and Molecular Biology, Mayo Clinic College of Medicine, Rochester, MN 55905, USA.

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.

*Corresponding author. 200 First Street SW, Guggenheim 13, Division of Oncology Research, Mayo Clinic College of Medicine, Rochester, MN 55905, USA. Telephone, 507-284-3124; fax, 507-284-3906; e-mail, karnitz.larry{at}mayo.edu

Citation: L. M. Karnitz, S. J. Felts, Cdc37 Regulation of the Kinome: When to Hold ‘Em and When to Fold ‘Em. Sci. STKE 2007, pe22 (2007).

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