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Dominant‐negative alleles of 14‐3‐3 proteins cause defects in actin organization and vesicle targeting in the yeast Saccharomyces cerevisiae
Author(s) -
Roth Dagmar,
Birkenfeld Jörg,
Betz Heinrich
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)01383-6
Subject(s) - exocytosis , microbiology and biotechnology , saccharomyces cerevisiae , vesicular transport protein , biology , vesicle , actin cytoskeleton , actin , cytoskeleton , munc 18 , yeast , genetics , secretion , biochemistry , cell , synaptic vesicle , membrane
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.