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The role of Far1p in linking the heterotrimeric G protein to polarity establishment proteins during yeast mating.

Science (New York, N.Y.) | Nov 20, 1998

http://www.ncbi.nlm.nih.gov/pubmed/9822386

Heterotrimeric guanosine triphosphate (GTP)-binding proteins (G proteins) determine tissue and cell polarity in a variety of organisms. In yeast, cells orient polarized growth toward the mating partner along a pheromone gradient by a mechanism that requires Far1p and Cdc24p. Far1p bound Gbetagamma and interacted with polarity establishment proteins, which organize the actin cytoskeleton. Cells containing mutated Far1p unable to bind Gbetagamma or polarity establishment proteins were defective for orienting growth toward their mating partner. In response to pheromones, Far1p moves from the nucleus to the cytoplasm. Thus, Far1p functions as an adaptor that recruits polarity establishment proteins to the site of extracellular signaling marked by Gbetagamma to polarize assembly of the cytoskeleton in a morphogenetic gradient.

Pubmed ID: 9822386 RIS Download

Mesh terms: Adaptor Proteins, Signal Transducing | Binding Sites | Carrier Proteins | Cell Cycle Proteins | Cell Membrane | Cell Nucleus | Cell Polarity | Cyclin-Dependent Kinase Inhibitor Proteins | Cytoskeleton | Fungal Proteins | GTP-Binding Protein beta Subunits | GTP-Binding Proteins | Guanine Nucleotide Exchange Factors | Heterotrimeric GTP-Binding Proteins | Models, Biological | Mutation | Peptides | Pheromones | Proto-Oncogene Proteins | Repressor Proteins | Saccharomyces cerevisiae | Saccharomyces cerevisiae Proteins | Signal Transduction | cdc42 GTP-Binding Protein, Saccharomyces cerevisiae

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Associated grants

  • Agency: NIGMS NIH HHS, Id: F32 GM017494
  • Agency: NIGMS NIH HHS, Id: GM48052
  • Agency: NIGMS NIH HHS, Id: GM57769
  • Agency: NIGMS NIH HHS, Id: R01 GM057769

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