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Vol. 14, Issue 12, 4958-4970, December 2003

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Interaction between a Ras and a Rho GTPase Couples Selection of a Growth Site to the Development of Cell Polarity in Yeast

Keith G. Kozminski ^*  , Laure Beven   ^¶, Elizabeth Angerman , Amy Hin Yan Tong ^|| #, Charles Boone ^|| #, and Hay-Oak Park  ^**

^* Departments of Biology and Cell Biology, University of Virginia, Charlottesville, Virginia 22904; Department of Molecular Genetics, The Ohio State University, Columbus, Ohio 43210; ^|| Banting and Best Department of Medical Research, University of Toronto, Toronto, Ontario, Canada M5G 1L6; and ^# Department of Medical Genetics and Microbiology, University of Toronto, Toronto, Ontario, Canada M5S 1A8

Submitted June 20, 2003; Revised July 25, 2003; Accepted July 28, 2003
Monitoring Editor: David Drubin

Polarized cell growth requires the coupling of a defined spatial site on the cell cortex to the apparatus that directs the establishment of cell polarity. In the budding yeast Saccharomyces cerevisiae, the Ras-family GTPase Rsr1p/Bud1p and its regulators select the proper site for bud emergence on the cell cortex. The Rho-family GTPase Cdc42p and its associated proteins then establish an axis of polarized growth by triggering an asymmetric organization of the actin cytoskeleton and secretory apparatus at the selected bud site. We explored whether a direct linkage exists between the Rsr1p/Bud1p and Cdc42p GTPases. Here we show specific genetic interactions between RSR1/BUD1 and particular cdc42 mutants defective in polarity establishment. We also show that Cdc42p coimmunoprecipitated with Rsr1p/Bud1p from yeast extracts. In vitro studies indicated a direct interaction between Rsr1p/Bud1p and Cdc42p, which was enhanced by Cdc24p, a guanine nucleotide exchange factor for Cdc42p. Our findings suggest that Cdc42p interacts directly with Rsr1p/Bud1p in vivo, providing a novel mechanism by which direct contact between a Ras-family GTPase and a Rho-family GTPase links the selection of a growth site to polarity establishment.

Part of this work was completed in the Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720.

^¶ Present address: UMR CNRS 6022, Universite deTechnologie de Compiegne, BP 20529, 60205 COMPIEGNE Cedex, France.

^** Corresponding author. E-mail address: park.294{at}osu.edu.

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