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Eukaryotic Cell, December 2006, p. 1950-1956, Vol. 5, No. 12
1535-9778/06/$08.00+0     doi:10.1128/EC.00256-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Regulation of the Nucleocytoplasmic Distribution of Snf1-Gal83 Protein Kinase{triangledown}

Kristina Hedbacker1 and Marian Carlson1,2*

Departments of Genetics and Development,1 Microbiology, Columbia University, New York, New York 100322

Received 11 August 2006/ Accepted 10 October 2006

Snf1 protein kinase containing the ß subunit Gal83 is localized in the cytoplasm during growth of Saccharomyces cerevisiae cells in abundant glucose and accumulates in the nucleus in response to glucose limitation. Nuclear localization of Snf1-Gal83 requires activation of the Snf1 catalytic subunit and depends on Gal83, but in the snf1{Delta} mutant, Gal83 exhibits glucose-regulated nuclear accumulation. We show here that the N terminus of Gal83, which is divergent from those of the other ß subunits, is necessary and sufficient for Snf1-independent, glucose-regulated localization. We identify a leucine-rich nuclear export signal in the N terminus and show that export depends on the Crm1 export receptor. We present evidence that catalytically inactive Snf1 promotes the cytoplasmic retention of Gal83 in glucose-grown cells through its interaction with the C terminus of Gal83; cytoplasmic localization of inactive Snf1-Gal83 maintains accessibility to the Snf1-activating kinases. Finally, we characterize the effects of glucose phosphorylation on localization. These studies define roles for Snf1 and Gal83 in determining the nucleocytoplasmic distribution of Snf1-Gal83 protein kinase.

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

{triangledown} Published ahead of print on 27 October 2006.

Eukaryotic Cell, December 2006, p. 1950-1956, Vol. 5, No. 12
1535-9778/06/$08.00+0     doi:10.1128/EC.00256-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Momcilovic, M., Iram, S. H., Liu, Y., Carlson, M. (2008). Roles of the Glycogen-binding Domain and Snf4 in Glucose Inhibition of SNF1 Protein Kinase. J. Biol. Chem. 283: 19521-19529 [Abstract] [Full Text]  
  • Rubenstein, E. M., McCartney, R. R., Zhang, C., Shokat, K. M., Shirra, M. K., Arndt, K. M., Schmidt, M. C. (2008). Access Denied: Snf1 Activation Loop Phosphorylation Is Controlled by Availability of the Phosphorylated Threonine 210 to the PP1 Phosphatase. J. Biol. Chem. 283: 222-230 [Abstract] [Full Text]  


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