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A more recent version of this article appeared on April 1, 2003
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Submitted on June 17, 2002
Revised on October 7, 2002
Accepted on December 4, 2002
1 Institute of Molecular Biology, University of Oregon, Eugene, OR 97403-1229 USA
2 Institute of Molecular Biology, University of Oregon, Eugene, OR 97403-1229 USA (present address: Intromex BioPharmaceuticals, Inc., #201-1618 Station Street Vancouver, B.C. V6A 2Y1)
3 Banting and Best Department of Medical Research, University of Toronto, 112 College St. Toronto ON, Canada M5G IL6; and Department of Medical Genetics and Microbiology, University of Toronto, 1 Kings College Circle, Toronto ON, Canada M5S 1A8
* Corresponding author. E-mail address: gsprague{at}molbio.uoregon.edu.
The p21-activated kinases (PAKs), Ste20p and Cla4p, carry out undefined function(s) 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. Here 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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