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Molecular and Cellular Biology, March 2004, p. 1836-1843, Vol. 24, No. 5
0270-7306/04/$08.00+0     DOI: 10.1128/MCB.24.5.1836-1843.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Cyclic AMP-Dependent Protein Kinase Regulates the Subcellular Localization of Snf1-Sip1 Protein Kinase

Kristina Hedbacker, Robert Townley, and Marian Carlson*

Department of Genetics and Development, Columbia University, New York, New York 10032

Received 8 July 2003/ Returned for modification 30 September 2003/ Accepted 21 November 2003

The Snf1/AMP-activated protein kinase family has diverse roles in cellular responses to metabolic stress. In Saccharomyces cerevisiae, Snf1 protein kinase has three isoforms of the ß subunit that confer versatility on the kinase and that exhibit distinct patterns of subcellular localization. The Sip1 ß subunit resides in the cytosol in glucose-grown cells and relocalizes to the vacuolar membrane in response to carbon stress. We show that translation of Sip1 initiates at the second ATG of the open reading frame, yielding a potential site for N myristoylation, and that mutation of the critical glycine abolishes relocalization. We further show that the cyclic AMP-dependent protein kinase (protein kinase A [PKA]) pathway maintains the cytoplasmic localization of Sip1 in glucose-grown cells. The Snf1 catalytic subunit also exhibits aberrant localization to the vacuolar membrane in PKA-deficient cells, indicating that PKA regulates the localization of Snf1-Sip1 protein kinase. These findings establish a novel mechanism of regulation of Snf1 protein kinase by the PKA pathway.

* Corresponding author. Mailing address: 701 W. 168th St., HSC922, New York, NY 10032. Phone: (212) 305-6314. Fax: (212) 305-1741. E-mail: mbc1{at}columbia.edu.

Molecular and Cellular Biology, March 2004, p. 1836-1843, Vol. 24, No. 5
0022-538X/04/$08.00+0     DOI: 10.1128/MCB.24.5.1836-1843.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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