This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Ren, M.
Right arrow Articles by Garrett, S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Ren, M.
Right arrow Articles by Garrett, S.

 Previous Article  |  Next Article 

Eukaryotic Cell, August 2007, p. 1363-1372, Vol. 6, No. 8
1535-9778/07/$08.00+0     doi:10.1128/EC.00165-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Alteration of the Protein Kinase Binding Domain Enhances Function of the Saccharomyces cerevisiae Molecular Chaperone Cdc37{triangledown}

Min Ren,1,2 Arti Santhanam,1,2 Paul Lee,3 Avrom Caplan,3 and Stephen Garrett2*

Graduate School of Biomedical Sciences,1 Department of Microbiology and Molecular Genetics, UMDNJ-New Jersey Medical School, Newark, New Jersey 07101,2 Department of Pharmacology and Systems Therapeutics, Mount Sinai School of Medicine, New York, New York 100293

Received 8 May 2007/ Accepted 2 June 2007

Cdc37 is a molecular chaperone that has a general function in the biogenesis of protein kinases. We identified mutations within the putative "protein kinase binding domain" of Cdc37 that alleviate the conditional growth defect of a strain containing a temperature-sensitive allele, tpk2(Ts), of the cyclic AMP-dependent protein kinase (PKA). These dominant mutations alleviate the temperature-sensitive growth defect by elevating PKA activity, as judged by their effects on PKA-regulated processes, localization and phosphorylation of the PKA effector Msn2, as well as in vitro PKA activity. Although the tpk2(Ts) growth defect is also alleviated by Cdc37 overproduction, the CDC37 dominant mutants contain wild-type Cdc37 protein levels. In addition, Saccharomyces cerevisiae Ste11 protein kinase has an elevated physical interaction with the altered Cdc37 protein. These results implicate specific amino-terminal residues in the interaction between Cdc37 and client protein kinases and provide further genetic and biochemical support for a model in which Cdc37 functions as a molecular chaperone for protein kinases.

* Corresponding author. Mailing address: Department of Microbiology and Molecular Genetics, UMDNJ-New Jersey Medical School, 225 Warren St., Newark, NJ 07101. Phone: (973) 972-4483, ext. 20698. Fax: (973) 972-8982. E-mail: garretst{at}umdnj.edu

{triangledown} Published ahead of print on 15 June 2007.

Eukaryotic Cell, August 2007, p. 1363-1372, Vol. 6, No. 8
1535-9778/07/$08.00+0     doi:10.1128/EC.00165-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.





Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»