Whiteway M S, Wu C, Leeuw T, Clark K, Fourest-Lieuvin A, Thomas D Y, Leberer E
Biotechnology Research Institute, National Research Council of Canada, Montreal, Quebec.
Science. 1995 Sep 15;269(5230):1572-5. doi: 10.1126/science.7667635.
The mating response pathway of the yeast Saccharomyces cerevisiae includes a heterotrimeric guanine nucleotide-binding protein (G protein) that activates a mitogen-activated protein MAP kinase cascade by an unknown mechanism. An amino-terminal fragment of the MAP kinase scaffold protein Ste5p that interfered with pheromone-induced cell cycle arrest was identified. A haploid-specific interaction between the amino terminus of Ste5p and the G protein beta subunit Ste4p was also detected in a two-hybrid assay, and the product of a signaling-defective allele of STE4 was defective in this interaction. In cells with a constitutively activated pheromone response pathway, epitope-tagged Ste4p was coimmunoprecipitated with Ste5p. Thus, association of the G protein and the MAP kinase cassette via the scaffolding protein Ste5p may transmit the G protein signal.
酿酒酵母的交配反应途径包括一种异源三聚体鸟嘌呤核苷酸结合蛋白(G蛋白),该蛋白通过未知机制激活丝裂原活化蛋白(MAP)激酶级联反应。我们鉴定出了MAP激酶支架蛋白Ste5p的一个氨基末端片段,它会干扰信息素诱导的细胞周期停滞。在双杂交试验中还检测到Ste5p氨基末端与G蛋白β亚基Ste4p之间的单倍体特异性相互作用,并且STE4信号缺陷等位基因的产物在这种相互作用中存在缺陷。在具有组成型激活的信息素反应途径的细胞中,表位标记的Ste4p与Ste5p共免疫沉淀。因此,G蛋白与MAP激酶盒通过支架蛋白Ste5p的结合可能会传递G蛋白信号。