Butty A C, Pryciak P M, Huang L S, Herskowitz I, Peter M
Swiss Institute for Experimental Cancer Research (ISREC), Chemin des Boveresses 155, 1066 Epalinges/VD, Switzerland.
Science. 1998 Nov 20;282(5393):1511-6. doi: 10.1126/science.282.5393.1511.
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.
异源三聚体鸟苷三磷酸（GTP）结合蛋白（G蛋白）在多种生物体中决定组织和细胞极性。在酵母中，细胞通过一种需要Far1p和Cdc24p的机制，沿着信息素梯度将极化生长导向交配伙伴。Far1p结合Gβγ并与组织肌动蛋白细胞骨架的极性建立蛋白相互作用。含有无法结合Gβγ或极性建立蛋白的突变Far1p的细胞，在将生长导向其交配伙伴方面存在缺陷。响应信息素时，Far1p从细胞核转移到细胞质。因此，Far1p作为一种衔接蛋白，将极性建立蛋白招募到由Gβγ标记的细胞外信号位点，以在形态发生梯度中使细胞骨架组装极化。
