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Originally published as MBC in Press, 10.1091/mbc.E08-12-1255 on May 20, 2009

Vol. 20, Issue 14, 3239-3250, July 15, 2009

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Regulation of Cell Polarity through Phosphorylation of Bni4 by Pho85 G1 Cyclin-dependent Kinases in Saccharomyces cerevisiae

Jian Zou*,{dagger}, Helena Friesen*,{dagger},{ddagger}, Jennifer Larson§, Dongqing Huang*,{dagger},{ddagger}, Mike Cox*,{dagger}, Kelly Tatchell§, and Brenda Andrews*,{dagger},{ddagger}

*Department of Molecular Genetics, {ddagger}Banting and Best Department of Medical Research, {dagger}Terrence Donnelly Centre for Cellular and Biomolecular Research, University of Toronto, Toronto, Ontario M5S 3E1, Canada; and §Department of Biochemistry and Molecular Biology, Louisiana State University Health Sciences Center, Shreveport, LA 71130

Submitted January 2, 2009; Revised May 11, 2009; Accepted May 13, 2009
Monitoring Editor: Fred Chang

InCytes from MBC

In the budding yeast Saccharomyces cerevisiae, the G1-specific cyclin-dependent kinases (Cdks) Cln1,2-Cdc28 and Pcl1,2-Pho85 are essential for ensuring that DNA replication and cell division are properly linked to cell polarity and bud morphogenesis. However, the redundancy of Cdks and cyclins means that identification of relevant Cdk substrates remains a significant challenge. We used array-based genetic screens (synthetic genetic array or SGA analysis) to dissect redundant pathways associated with G1 cyclins and identified Bni4 as a substrate of the Pcl1- and Pcl2-Pho85 kinases. BNI4 encodes an adaptor protein that targets several proteins to the bud neck. Deletion of BNI4 results in severe growth defects in the absence of the Cdc28 cyclins Cln1 and Cln2, and overexpression of BNI4 is toxic in yeast cells lacking the Pho85 cyclins Pcl1 and Pcl2. Phosphorylation of Bni4 by Pcl-Pho85 is necessary for its localization to the bud neck, and the bud neck structure can be disrupted by overexpressing BNI4 in pcl1{Delta}pcl2{Delta} mutant cells. Our data suggest that misregulated Bni4 may bind in an uncontrolled manner to an essential component that resides at the bud neck, causing catastrophic morphogenesis defects.

This was published online ahead of print in MBC in Press (http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E08-12-1255) on May 20, 2009.

Address correspondence to: Brenda Andrews (brenda.andrews{at}utoronto.ca)

Abbreviations used: Cdk, cyclin-dependent kinase; SDL, synthetic dosage lethal; SL, synthetic lethal; WT, wild type.


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Mol. Biol. Cell 2009 20: 3169. [PDF]  





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