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Vol. 14, Issue 5, 2128-2141, May 2003
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* National Institute of Diabetes and Digestive and Kidney Diseases, Laboratory
of Biochemistry and Genetics, Bethesda, Maryland 20892;
National Heart, Lung and Blood Institute, Laboratory of Cell Biology,
Bethesda, Maryland 20892
Submitted August 30, 2002;
Revised December 12, 2002;
Accepted December 27, 2002
Monitoring Editor: David Drubin
CLA4, encoding a protein kinase of the PAK type, and CDC11, encoding a septin, were isolated in a screen for synthetic lethality with CHS3, which encodes the chitin synthase III catalytic moiety. Although Ste20p shares some essential function with Cla4p, it did not show synthetic lethality with Chs3p. cla4 and cdc11 mutants exhibited similar morphological and septin localization defects, including aberrant and ectopic septa. Myo1p, which requires septins for localization, formed abnormally wide rings in cla4 mutants. In cultures started with unbudded cells, an inhibitor of Chs3p activity, nikkomycin Z, aggravated the abnormalities of cla4 and cdc11 mutants and gave rise to enlarged necks at the mother-bud junction, leading to cell death. It is concluded that Cla4p is required for the correct localization and/or assembly of the septin ring and that both the septin ring and the Chs3p-requiring chitin ring at the mother-bud neck cooperate in maintaining the neck constricted throughout the cell cycle, a vital function in budding yeast.
Present address: Molecular Neurobiology Branch, Charles River
Laboratories/National Institute on Drug Abuse, Room 306, 5500 Nathan Shock
Drive, Baltimore, MD 21224.
Corresponding author. E-mail address:
enricoc{at}bdg10.niddk.nih.gov.
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