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

FEBS Lett. 1999 Nov 5;460(3):411-6. doi: 10.1016/s0014-5793(99)01383-6.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 14-3-3 Proteins
  • Actins / chemistry
  • Actins / genetics
  • Actins / physiology*
  • Alleles*
  • Cell Compartmentation / genetics
  • Cytoplasmic Granules / physiology*
  • Genes, Dominant
  • Mutation / genetics
  • Phospholipases A / genetics
  • Phosphopyruvate Hydratase / genetics
  • Protein Biosynthesis
  • Protein Kinase C / antagonists & inhibitors
  • Proteins / genetics*
  • Saccharomyces cerevisiae / genetics*
  • Saccharomyces cerevisiae / metabolism
  • Tyrosine 3-Monooxygenase*

Substances

  • 14-3-3 Proteins
  • Actins
  • Proteins
  • Tyrosine 3-Monooxygenase
  • Protein Kinase C
  • Phospholipases A
  • Phosphopyruvate Hydratase