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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. Leeaa 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
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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