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Vol. 14, Issue 4, 1501-1516, April 2003

Synthetic Lethal Analysis Implicates Ste20p, a p21-activated Protein Kinase, in Polarisome Activation

April S. Goehring,^* David A. Mitchell,^* Amy Hin Yan Tong,^§ Megan E. Keniry,^* Charles Boone,^§ and George F. Sprague Jr.^*

 ^*Institute of Molecular Biology, University of Oregon, Eugene, Oregon 97403-1229;  Banting and Best Department of Medical Research, University of Toronto, Toronto, Ontario, Canada M5G IL6; and  ^§Department of Medical Genetics and Microbiology, University of Toronto, Toronto, Ontario, Canada M5S 1A8

The p21-activated kinases Ste20p and Cla4p carry out undefined functions that are essential for viability during budding in Saccharomyces cerevisiae. To gain insight into the roles of Ste20p, we have used a synthetic lethal mutant screen to identify additional genes that are required in the absence of Cla4p. Altogether, we identified 65 genes, including genes with roles in cell polarity, mitosis, and cell wall maintenance. Herein, we focus on a set that defines a function carried out by Bni1p and several of its interacting proteins. We found that Bni1p and a group of proteins that complex with Bni1p (Bud6p, Spa2p, and Pea2p) are essential in a cla4 mutant background. Bni1p, Bud6p, Spa2, and Pea2p are members of a group of polarity determining proteins referred to as the polarisome. Loss of polarisome proteins from a cla4 strain causes cells to form elongated buds that have mislocalized septin rings. In contrast, other proteins that interact with or functionally associate with Bni1p and have roles in nuclear migration and cytokinesis, including Num1p and Hof1p, are not essential in the absence of Cla4p. Finally, we have found that Bni1p is phosphorylated in vivo, and a substantial portion of this phosphorylation is dependent on STE20. Together, these results suggest that one function of Ste20p may be to activate the polarisome complex by phosphorylation of Bni1p.

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The online version of this article contains supplemental tabular material. The online version of the article is available at www.molbiolcell.org.

Current address: Intromex BioPharmaceuticals, Inc., #201-1618 Station St., Vancouver, BC, Canada V6A 2Y1.

Corresponding author. E-mail address: gsprague{at}molbio.uoregon.edu.

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Molecular Biology of the Cell
Vol. 14, 1501-1516, April 2003
Copyright © 2003 by The American Society for Cell Biology

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