The Role of Far1p in Linking the Heterotrimeric G Protein to Polarity Establishment Proteins During Yeast Mating

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Science  20 Nov 1998:
Vol. 282, Issue 5393, pp. 1511-1516
DOI: 10.1126/science.282.5393.1511

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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 Gβγ and interacted with polarity establishment proteins, which organize the actin cytoskeleton. Cells containing mutated Far1p unable to bind Gβγ 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 Gβγ to polarize assembly of the cytoskeleton in a morphogenetic gradient.

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