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J. Biol. Chem., Vol. 283, Issue 4, 1962-1973, January 25, 2008

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Modulation of Yeast Sln1 Kinase Activity by the Ccw12 Cell Wall Protein^*

Sandhya S. Narang, Cheryl L. Malone, Robert J. Deschenes, and Jan S. Fassler¹

From the Department of Biological Sciences, University of Iowa, Iowa City, Iowa 52242 and the Department of Biochemistry, Medical College of Wisconsin, Milwaukee, Wisconsin 53226

The yeast Sln1p sensor kinase is best known as an osmosensor involved in the regulation of the hyperosmolarity glycerol mitogen-activated protein kinase cascade. Down-regulation of Sln1 kinase activity occurs under hypertonic conditions and leads to phosphorylation of the Hog1p mitogen-activated protein kinase and increased osmotic stress-response gene expression. Conditions leading to kinase up-regulation include osmotic imbalance caused by glycerol retention in the glycerol channel mutant, fps1 (Tao, W., Deschenes, R. J., and Fassler, J. S. (1999) J. Biol. Chem. 274, 360–367). The hypothesis that Sln1p kinase activity is responsive to turgor was first suggested by the increased Sln1p kinase activity in mutants lacking Fps1p in which glycerol accumulation leads to water uptake. Also consistent with the turgor hypothesis is the observation that reduced turgor caused by treatment of cells with nystatin, a drug that increases membrane permeability and causes cell shrinkage, reduced Sln1p kinase activity (Tao, W., Deschenes, R. J., and Fassler, J. S. (1999) J. Biol. Chem. 274, 360–367; Reiser, V., Raitt, D. C., and Saito, H. (2003) J. Cell Biol. 161, 1035–1040). The turgor hypothesis is revisited here in the context of the identification and characterization of the cell wall gene, CCW12, as a determinant of Sln1p activity. Results of this analysis suggest that the activity of the plasma membrane localized Sln1p is affected by the presence or absence of specific outer cell wall proteins and that this effect is independent of turgor.

Received for publication, August 17, 2007 , and in revised form, November 12, 2007.

^* This work was supported by the National Institutes of Health Grant GM56719 and by a predoctoral fellowship from the Center for Biocatalysis and Bioprocessing (to S. S. N.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ To whom correspondence should be addressed: 202 BBE, Dept. of Biological Sciences, University of Iowa, Iowa City, IA 52242. Tel.: 319-335-1542; Fax: 319-335-1069; E-mail: jan-fassler{at}uiowa.edu.

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