Dominant‐negative alleles of 14‐3‐3 proteins cause defects in actin organization and vesicle targeting in the yeast Saccharomyces cerevisiae

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Abstract
14‐3‐3 Proteins are thought to function as adapters in signaling complexes [1,2], thereby participating in cellular processes including vesicle trafficking and exocytosis [3,4]. To delineate further the function of 14‐3‐3 proteins during vesicle trafficking, we generated dominant‐negative alleles of the two 14‐3‐3 homologues, Bmh1p and Bmh2p, in budding yeast and analyzed their phenotype in respect to exocytosis. Cells overexpressing the carboxy‐terminal region of Bmh2p failed to polarize vesicular transport although bulk exocytosis remained unaffected and showed a disrupted actin cytoskeleton. Our data suggest that 14‐3‐3 proteins may act primarily on the actin cytoskeleton to regulate vesicle targeting.