Marcus S, Polverino A, Chang E, Robbins D, Cobb M H, Wigler M H
Cold Spring Harbor Laboratory, NY 11724, USA.
Proc Natl Acad Sci U S A. 1995 Jun 20;92(13):6180-4. doi: 10.1073/pnas.92.13.6180.
We describe a protein kinase, Shk1, from the fission yeast Schizosaccharomyces pombe, which is structurally related to the Saccharomyces cerevisiae Ste20 and mammalian p65PAK protein kinases. We provide genetic evidence for physical and functional interaction between Shk1 and the Cdc42 GTP-binding protein required for normal cell morphology and mating in S. pombe. We further show that expression of the STE20 gene complements the shk1 null mutation and that Shk1 is capable of signaling to the pheromone-responsive mitogen-activated protein kinase cascade in S. cerevisiae. Our results lead us to propose that signaling modules composed of small GTP-binding proteins and protein kinases related to Shk1, Ste20, and p65PAK, are highly conserved in evolution and participate in both cytoskeletal functions and mitogen-activated protein kinase signaling pathways.
我们描述了一种来自裂殖酵母粟酒裂殖酵母的蛋白激酶Shk1，它在结构上与酿酒酵母的Ste20和哺乳动物的p65PAK蛋白激酶相关。我们提供了Shk1与粟酒裂殖酵母中正常细胞形态和交配所需的Cdc42 GTP结合蛋白之间存在物理和功能相互作用的遗传学证据。我们进一步表明，STE20基因的表达可弥补shk1缺失突变，并且Shk1能够向酿酒酵母中的信息素应答促分裂原活化蛋白激酶级联发出信号。我们的结果使我们提出，由小GTP结合蛋白和与Shk1、Ste20和p65PAK相关的蛋白激酶组成的信号模块在进化中高度保守，并参与细胞骨架功能和促分裂原活化蛋白激酶信号通路。
