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J. Biol. Chem., Vol. 283, Issue 21, 14205-14212, May 23, 2008

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Regulation of Gic2 Localization and Function by Phosphatidylinositol 4,5-Bisphosphate during the Establishment of Cell Polarity in Budding Yeast^*

Kelly Orlando¹², Jian Zhang¹, Xiaoyu Zhang, Peng Yue, Teresa Chiang, Erfei Bi, and Wei Guo³

From the Departments of Biology and Cell and Developmental Biology, University of Pennsylvania, Philadelphia, Pennsylvania 19104-6018

Establishment of cell polarity is important for a wide range of biological processes, from asymmetric cell growth in budding yeast to neurite formation in neurons. In the yeast Saccharomyces cerevisiae, the small GTPase Cdc42 controls polarized actin organization and exocytosis toward the bud. Gic2, a Cdc42 effector, is targeted to the bud tip and plays an important role in early bud formation. The GTP-bound Cdc42 interacts with Gic2 through the Cdc42/Rac interactive binding domain located at the N terminus of Gic2 and activates Gic2 during bud emergence. Here we identify a polybasic region in Gic2 adjacent to the Cdc42/Rac interactive binding domain that directly interacts with phosphatidylinositol 4,5-bisphosphate in the plasma membrane. We demonstrate that this interaction is necessary for the polarized localization of Gic2 to the bud tip and is important for the function of Gic2 in cell polarization. We propose that phosphatidylinositol 4,5-bisphosphate and Cdc42 act in concert to regulate polarized localization and function of Gic2 during polarized cell growth in the budding yeast.

Received for publication, October 2, 2007 , and in revised form, March 31, 2008.

^* This work was supported, in whole or in part, by National Institutes of Health Grant GM64690. This work was also supported by the Pew Scholars Program in Biomedical Sciences (to W. G.) and NIH Grant GM59216 (to E. B.). 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.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Fig. S1.

¹ Both authors contributed equally to this work.

² Supported by NIGMS, NIH Grant F32GM082012.

³ To whom correspondence should be addressed. Tel.: 215-898-9384; Fax: 215-898-8780; E-mail: guowei{at}sas.upenn.edu.

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