Dominant-negative alleles of 14-3-3 proteins cause defects in actin organization and vesicle targeting in the yeast Saccharomyces cerevisiae.
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.
Roth
D
D
Department of Neurochemistry, Max-Planck-Institute for Brain Research, Deutschordenstr. 46, 60528, Frankfurt, Germany. roth@mpih-frankfurt.mpg.de
Birkenfeld
J
J
Betz
H
H
D048948:14-3-3 Proteins; D000199:Actins / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D000483:Alleles; D002451:Cell Compartmentation / Q000235:genetics; D003594:Cytoplasmic Granules / Q000502:physiology*; D005799:Genes, Dominant; D009154:Mutation / Q000235:genetics; D010741:Phospholipases A / Q000235:genetics; D010751:Phosphopyruvate Hydratase / Q000235:genetics; D014176:Protein Biosynthesis; D011493:Protein Kinase C / Q000037:antagonists & inhibitors; D011506:Proteins / Q000235:genetics*; D012441:Saccharomyces cerevisiae / Q000235:genetics* / Q000378:metabolism; D014446:Tyrosine 3-Monooxygenase
D048948:14-3-3 Proteins; D000199:Actins; D011506:Proteins; D014446:Tyrosine 3-Monooxygenase; D011493:Protein Kinase C; D010741:Phospholipases A; D010751:Phosphopyruvate Hydratase