Selective Regulation of MAP Kinase Signaling by an Endomembrane Phosphatidylinositol 4-Kinase

被引:14
作者
Cappell, Steven D. [2 ]
Dohlman, Henrik G. [1 ,2 ]
机构
[1] Univ N Carolina, Dept Biochem & Biophys, Chapel Hill, NC 27599 USA
[2] Univ N Carolina, Dept Pharmacol, Chapel Hill, NC 27599 USA
基金
美国国家卫生研究院;
关键词
YEAST SACCHAROMYCES-CEREVISIAE; PHEROMONE RESPONSE PATHWAY; G-BETA-GAMMA; G-PROTEIN SUBUNITS; FILAMENTOUS GROWTH; PLASMA-MEMBRANE; ADAPTER PROTEIN; TRANSDUCTION PATHWAY; SCAFFOLD PROTEIN; BINDING DOMAINS;
D O I
10.1074/jbc.M110.195073
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Multiple MAP kinase pathways share components yet initiate distinct biological processes. Signaling fidelity can be maintained by scaffold proteins and restriction of signaling complexes to discreet subcellular locations. For example, the yeast MAP kinase scaffold Ste5 binds to phospholipids produced at the plasma membrane and promotes selective MAP kinase activation. Here we show that Pik1, a phosphatidylinositol 4-kinase that localizes primarily to the Golgi, also regulates MAP kinase specificity but does so independently of Ste5. Pik1 is required for full activation of the MAP kinases Fus3 and Hog1 and represses activation of Kss1. Further, we show by genetic epistasis analysis that Pik1 likely regulates Ste11 and Ste50, components shared by all three MAP kinase pathways, through their interaction with the scaffold protein Opy2. These findings reveal a new regulator of signaling specificity functioning at endomembranes rather than at the plasma membrane.
引用
收藏
页码:14852 / 14860
页数:9
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