Std1p (Msn3p) positively regulates the Snf1 kinase in Saccharomyces cerevisiae.
Std1p (Msn3p) positively regulates the Snf1 kinase in Saccharomyces cerevisiae.
复制标题
Std1p (Msn3p) 对酿酒酵母中的 Snf1 激酶具有正向调节作用。
DOI：
10.1093/genetics/163.2.507
复制
发表时间：
2003
期刊：
影响因子：
3.3
通讯作者：
Carlson,Marian
中科院分区：
文献类型：
--
作者：
Kuchin,Sergei;Vyas,ValmikK;Kanter,Ellen;Hong,Seung-Pyo;Carlson,Marian
The Snf1 protein kinase of the glucose signaling pathway inSaccharomyces cerevisiaeis regulated by an autoinhibitory interaction between the regulatory and catalytic domains of Snf1p. Transitions between the autoinhibited and active states are controlled by an upstream kinase and the Reg1p-Glc7p protein phosphatase 1. Previous studies suggested that Snf1 kinase activity is also modulated by Std1p (Msn3p), which interacts physically with Snf1p and also interacts with glucose sensors. Here we address the relationship between Std1p and the Snf1 kinase. Two-hybrid assays showed that Std1p interacts with the catalytic domain of Snf1p, and analysis of mutant kinases suggested that this interaction is incompatible with the autoinhibitory interaction of the regulatory and catalytic domains. Overexpression of Std1p increased the two-hybrid interaction of Snf1p with its activating subunit Snf4p, which is diagnostic of an open, uninhibited conformation of the kinase complex. Overexpression of Std1p elevated Snf1 kinase activity in bothin vitroandin vivoassays. These findings suggest that Std1p stimulates the Snf1 kinase by an interaction with the catalytic domain that antagonizes autoinhibition and promotes an active conformation of the kinase.
