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J. Biol. Chem., Vol. 282, Issue 22, 15946-15953, June 1, 2007

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Up-regulation of the Cell Integrity Pathway in Saccharomyces cerevisiae Suppresses Temperature Sensitivity of the pgs1 Mutant^*

From the Department of Biological Sciences, Wayne State University, Detroit, Michigan 48202

We have previously shown that mutants in the cardiolipin (CL) pathway exhibit temperature-sensitive growth defects that are not associated with mitochondrial dysfunction. The pgs1 mutant, lacking the first enzyme of the CL pathway, phosphatidylglycerolphosphate synthase (Pgs1p), has a defective cell wall due to decreased -1,3-glucan (Zhong, Q., Gvozdenovic-Jeremic, J., Webster, P., Zhou, J., and Greenberg, M. L. (2005) Mol. Biol. Cell 16, 665–675). Disruption of KRE5, a gene involved in cell wall biogenesis, restores -1,3-glucan synthesis and suppresses pgs1 temperature sensitivity. To gain insight into the mechanisms underlying the cell wall defect in pgs1, we show in the current report that pgs1 cells have reduced glucan synthase activity and diminished levels of Fks1p, the glucan synthase catalytic subunit. In addition, activation of Slt2p, the downstream effector of the protein kinase C (PKC)-activated cell integrity pathway, was defective in pgs1. The kre5^W1166X suppressor restored Slt2p activation and dramatically increased (>10-fold) mRNA levels of FKS2, the alternate catalytic subunit of glucan synthase, partially restoring glucan synthase activity. Consistent with these results, up-regulation of PKC-Slt2 signaling and overexpression of FKS1 or FKS2 alleviated sensitivity of pgs1 to cell wall-perturbing agents and restored growth at elevated temperature. These findings demonstrate that functional Pgs1p is essential for cell wall biogenesis and activation of the PKC-Slt2 signaling pathway.

Received for publication, February 5, 2007 , and in revised form, March 19, 2007.

^* This work was supported by National Institutes of Health Grant HL62263 and by a grant from the Barth Syndrome Foundation. 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 These two authors contributed equally to this work.

² Present address: Dept. of Cancer Biology, Dana Farber Cancer Institute, Harvard Medical School, 44 Binney St., Boston, MA.

³ To whom correspondence should be addressed: Dept. of Biological Sciences, Wayne State University, Detroit, MI 48202. Tel.: 313-577-5202; Fax: 313-577-6891; E-mail: MLGREEN{at}sun.science.wayne.edu.

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