Valtz N, Peter M, Herskowitz I
Department of Biochemistry and Biophysics, University of California, San Francisco 94143-0448, USA.
J Cell Biol. 1995 Nov;131(4):863-73. doi: 10.1083/jcb.131.4.863.
Cell polarization involves specifying an area on the cell surface and organizing the cytoskeleton towards that landmark. The mechanisms by which external signals are translated into internal landmarks for polarization are poorly understood. The yeast Saccharomyces cerevisiae exhibits polarized growth during mating: the actin cytoskeleton of each cell polarizes towards its partner, presumably to allow efficient cell fusion. The external signal which determines the landmark for polarization is thought to be a gradient of peptide pheromone released by the mating partner. Here we described mutants that exhibit random polarization. Using two assays, including a direct microscope assay for orientation (Segall, J. 1993. Proc. Natl. Acad. Sci. USA. 90:8332-8337), we show that these mutants cannot locate the source of a pheromone gradient although they are able to organize their cytoskeleton. These mutants appear to be defective in mating because they are unable to locate the mating partner. They carry mutations of the FAR1 gene, denoted far1-s, and identify a new function for the Far1 protein. Its other known function is to promote cell cycle arrest during mating by inhibiting a cyclin-dependent kinase (Peter, M., and I. Herskowitz. 1994. Science (Wash. DC). 265:1228-1232). The far1-s mutants exhibit normal cell cycle arrest in response to pheromone, which suggests that Far1 protein plays two distinct roles in mating: one in cell cycle arrest and the other in orientation towards the mating partner.
细胞极化涉及在细胞表面确定一个区域,并朝着该标志组织细胞骨架。外界信号转化为极化内部标志的机制目前了解甚少。酿酒酵母在交配过程中表现出极化生长:每个细胞的肌动蛋白细胞骨架朝着其伴侣极化,大概是为了实现高效的细胞融合。据认为,决定极化标志的外界信号是交配伴侣释放的肽类信息素梯度。在此,我们描述了表现出随机极化的突变体。通过两种检测方法,包括一种用于定向的直接显微镜检测法(Segall, J. 1993. Proc. Natl. Acad. Sci. USA. 90:8332 - 8337),我们发现这些突变体虽然能够组织其细胞骨架,但无法定位信息素梯度的来源。这些突变体似乎在交配方面存在缺陷,因为它们无法找到交配伴侣。它们携带FAR1基因的突变,记为far1 - s,并确定了Far1蛋白的一种新功能。其另一个已知功能是通过抑制细胞周期蛋白依赖性激酶在交配过程中促进细胞周期停滞(Peter, M., and I. Herskowitz. 1994. Science (Wash. DC). 265:1228 - 1232)。far1 - s突变体对信息素表现出正常的细胞周期停滞,这表明Far1蛋白在交配过程中发挥两种不同的作用:一种是在细胞周期停滞方面,另一种是在朝着交配伴侣的定向方面。