A conserved protein interaction network involving the yeast MAP kinases Fus3 and Kss1

被引：62

作者：

Kusari, AB ^{[1
]}

Molina, DM ^{[1
]}

Sabbagh, W ^{[1
]}

Lau, CS ^{[1
]}

Bardwell, L ^{[1
]}

机构：

[1] Univ Calif Irvine, Dept Dev & Cell Biol, Irvine, CA 92697 USA

来源：

JOURNAL OF CELL BIOLOGY | 2004年 / 164卷 / 02期

关键词：

mitogen-activated protein kinases; signal transduction; phosphorylation; binding sites; protein binding;

D O I：

10.1083/jcb.200310021

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

The Saccharomyces cerevisiae mitogen-activated protein kinases (MAPKs) Fus3 and Kss1 bind to multiple regulators and substrates. We show that mutations in a conserved docking site in these MAPKs (the CD/7rn region) disrupt binding to an important subset of their binding partners, including the Ste7 MAPK kinase, the Ste5 adaptor/scaffold protein, and the Dig1 and Dig2 transcriptional repressors. Supporting the possibility that Ste5 and Ste7 bind to the same region of the MAPKs, they partially competed for Fus3 binding. In vivo, some of the MAPK mutants displayed reduced Ste7-dependent phosphorylation, and all of them exhibited multiple defects in mating and pheromone response. The Kss1 mutants were also defective in Kss1-imposed repression of Ste12. We conclude that MAPKs contain a structurally and functionally conserved docking site that mediates an overall positively acting network of interactions with cognate docking sites on their regulators and substrates. Key features of this interaction network appear to have been conserved from yeast to humans.

引用

页码：267 / 277

页数：11

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