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Rho1 GTP酶对酵母蛋白激酶C的激活作用。

Activation of yeast protein kinase C by Rho1 GTPase.

作者信息

Kamada Y, Qadota H, Python C P, Anraku Y, Ohya Y, Levin D E

机构信息

Department of Biochemisty, Johns Hopkins University School of Public Health, Baltimore, Maryland 21205, USA.

出版信息

J Biol Chem. 1996 Apr 19;271(16):9193-6. doi: 10.1074/jbc.271.16.9193.

Abstract

We have investigated the role of the essential Rho1 GTPase in cell integrity signaling in budding yeast. Conditional rho1 mutants display a cell lysis defect that is similar to that of mutants in the cell integrity signaling pathway mediated by protein kinase C (Pkc1), which is suppressed by overexpression of Pkc1.rho1 mutants are also impaired in pathway activation in response to growth at elevated temperature. Pkc1 co-immunoprecipitates with Rho1 in yeast extracts, and recombinant Rho1 associates with Pkc1 in vitro in a GTP-dependent manner. Recombinant Rho1 confers upon Pkc1 the ability to be stimulated by phosphatidylserine, indicating that Rho1 controls signal transmission through Pkc1.

摘要

我们研究了必需的Rho1 GTP酶在芽殖酵母细胞完整性信号传导中的作用。条件性rho1突变体表现出细胞裂解缺陷,这与蛋白激酶C(Pkc1)介导的细胞完整性信号通路中的突变体相似,Pkc1的过表达可抑制该缺陷。rho1突变体在高温下生长时的通路激活也受损。在酵母提取物中,Pkc1与Rho1共免疫沉淀,并且重组Rho1在体外以GTP依赖的方式与Pkc1结合。重组Rho1赋予Pkc1被磷脂酰丝氨酸刺激的能力,表明Rho1通过Pkc1控制信号传递。

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