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The yeast Ste20 protein kinase is involved in pheromone response. Mammalian homologs of Ste20 exist, but their function remains unknown. We identified a novel yeast STE20 homolog, CLA4, in a screen for mutations lethal in the absence of the G1 cyclins Cln1 and Cln2. Cla4 is involved in budding and cytokinesis and interacts with Cdc42, a GTPase required for polarized cell growth. Despite a cytokinesis defect, cla4 mutants are viable. However, double cla4 ste20 mutants cannot maintain septin rings at the bud neck and cannot undergo cytokinesis. Mutations in CDC12, which encodes one of the septins, were found in the same screen. Cla4 and Ste20 kinases apparently share a function in localizing cell growth with respect to the septin ring.

Type

Journal article

Journal

Genes Dev

Publication Date

01/08/1995

Volume

9

Pages

1817 - 1830

Keywords

Amino Acid Sequence, Cell Compartmentation, Cell Cycle Proteins, Cell Division, Cell Polarity, Cyclins, Fungal Proteins, GTP Phosphohydrolases, Genes, Fungal, Intracellular Signaling Peptides and Proteins, MAP Kinase Kinase Kinases, Molecular Sequence Data, Pheromones, Protein Kinase C, Protein-Serine-Threonine Kinases, Saccharomyces cerevisiae Proteins, Sequence Homology, Amino Acid, Signal Transduction, Yeasts