Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.


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


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}

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).

Read the Full Text

Canonical and Kinase Activity-Independent Mechanisms for Extracellular Signal-Regulated Kinase 5 (ERK5) Nuclear Translocation Require Dissociation of Hsp90 from the ERK5-Cdc37 Complex.
T. Erazo, A. Moreno, G. Ruiz-Babot, A. Rodriguez-Asiain, N. A. Morrice, J. Espadamala, J. R. Bayascas, N. Gomez, and J. M. Lizcano (2013)
Mol. Cell. Biol. 33, 1671-1686
   Abstract »    Full Text »    PDF »
Specific Regulation of Noncanonical p38{alpha} Activation by Hsp90-Cdc37 Chaperone Complex in Cardiomyocyte.
A. Ota, J. Zhang, P. Ping, J. Han, and Y. Wang (2010)
Circ. Res. 106, 1404-1412
   Abstract »    Full Text »    PDF »
The Chaperones Hsp90 and Cdc37 Mediate the Maturation and Stabilization of Protein Kinase C through a Conserved PXXP Motif in the C-terminal Tail.
C. M. Gould, N. Kannan, S. S. Taylor, and A. C. Newton (2009)
J. Biol. Chem. 284, 4921-4935
   Abstract »    Full Text »    PDF »
HDAC6 inhibition enhances 17-AAG-mediated abrogation of hsp90 chaperone function in human leukemia cells.
R. Rao, W. Fiskus, Y. Yang, P. Lee, R. Joshi, P. Fernandez, A. Mandawat, P. Atadja, J. E. Bradner, and K. Bhalla (2008)
Blood 112, 1886-1893
   Abstract »    Full Text »    PDF »

To Advertise     Find Products

Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882