Genetics, Vol. 163, 21-33, January 2003, Copyright © 2003

Loss of CDC5 Function in Saccharomyces cerevisiae Leads to Defects in Swe1p Regulation and Bfa1p/Bub2p-Independent Cytokinesis

Chong Jin Parka, Sukgil Songa, Philip R. Leea, Wenying Shoub, Raymond J. Deshaiesb,c, and Kyung S. Leea
a Laboratory of Metabolism, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892
b Division of Biology, California Institute of Technology, Pasadena, California 91125
c Howard Hughes Medical Institute, California Institute of Technology, Pasadena, California 91125

Corresponding author: Kyung S. Lee, National Cancer Institute, NIH, 9000 Rockville Pike, Bldg. 37, Rm. 3D25, Bethesda, MD 20892., kyunglee{at}pop.nci.nih.gov (E-mail)

Communicating editor: N. A. JENKINS

In many organisms, polo kinases appear to play multiple roles during M-phase progression. To provide new insights into the function of budding yeast polo kinase Cdc5p, we generated novel temperature-sensitive cdc5 mutants by mutagenizing the C-terminal domain. Here we show that, at a semipermissive temperature, the cdc5-3 mutant exhibited a synergistic bud elongation and growth defect with loss of HSL1, a component important for normal G2/M transition. Loss of SWE1, which phosphorylates and inactivates the budding yeast Cdk1 homolog Cdc28p, suppressed the cdc5-3 hsl1{Delta} defect, suggesting that Cdc5p functions at a point upstream of Swe1p. In addition, the cdc5-4 and cdc5-7 mutants exhibited chained cell morphologies with shared cytoplasms between the connected cell bodies, indicating a cytokinetic defect. Close examination of these mutants revealed delayed septin assembly at the incipient bud site and loosely organized septin rings at the mother-bud neck. Components in the mitotic exit network (MEN) play important roles in normal cytokinesis. However, loss of BFA1 or BUB2, negative regulators of the MEN, failed to remedy the cytokinetic defect of these mutants, indicating that Cdc5p promotes cytokinesis independently of Bfa1p and Bub2p. Thus, Cdc5p contributes to the activation of the Swe1p-dependent Cdc28p/Clb pathway, normal septin function, and cytokinesis.





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