Molecular Mimicry Regulates ABA Signaling by SnRK2 Kinases and PP2C Phosphatases

被引：438

作者：

Soon, Fen-Fen ^{[1
,2
]}

Ng, Ley-Moy ^{[1
,2
]}

Zhou, X. Edward ^{[1
]}

West, Graham M. ^{[3
]}

Kovach, Amanda ^{[1
]}

Tan, M. H. Eileen ^{[1
,2
]}

Suino-Powell, Kelly M. ^{[1
]}

He, Yuanzheng ^{[1
]}

Xu, Yong ^{[1
]}

Chalmers, Michael J. ^{[3
]}

Brunzelle, Joseph S. ^{[4
]}

Zhang, Huiming ^{[5
]}

Yang, Huaiyu ^{[6
]}

Jiang, Hualiang ^{[6
]}

Li, Jun ^{[1
,2
]}

Yong, Eu-Leong ^{[2
]}

Cutler, Sean ^{[7
]}

Zhu, Jian-Kang ^{[5
]}

Griffin, Patrick R. ^{[3
]}

Melcher, Karsten ^{[1
]}

Xu, H. Eric ^{[1
,8
]}

机构：

[1] Van Andel Res Inst, Lab Struct Sci, Grand Rapids, MI 49503 USA

[2] Natl Univ Singapore, Dept Obstet & Gynecol, Yong Loo Lin Sch Med, Natl Univ Hosp, Singapore 119228, Singapore

[3] Scripps Res Inst, Dept Mol Therapeut, Translat Res Inst, Jupiter, FL 33458 USA

[4] Northwestern Univ, Dept Mol Pharmacol & Biol Chem, Life Sci Collaborat Access Team, Synchrotron Res Ctr, Argonne, IL 60439 USA

[5] Purdue Univ, Dept Hort & Landscape Architecture, W Lafayette, IN 47907 USA

[6] Chinese Acad Sci, Ctr Drug Discovery & Design, State Key Lab Drug Res, Shanghai Inst Mat Med, Shanghai 201203, Peoples R China

[7] Univ Calif Riverside, Dept Bot & Plant Sci, Riverside, CA 92521 USA

[8] Chinese Acad Sci, VARI SIMM Ctr, Ctr Struct & Funct Drug Targets, State Key Lab Drug Res,Shanghai Inst Mat Med, Shanghai 201203, Peoples R China

来源：

SCIENCE | 2012年 / 335卷 / 6064期

基金：

美国国家科学基金会;

关键词：

2C PROTEIN PHOSPHATASES; ABSCISIC-ACID; GUARD-CELLS; ACTIVATION; PHOSPHORYLATION; ARABIDOPSIS; MECHANISMS; CHANNEL; OST1; PAIR;

D O I：

10.1126/science.1215106

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Abscisic acid (ABA) is an essential hormone for plants to survive environmental stresses. At the center of the ABA signaling network is a subfamily of type 2C protein phosphatases (PP2Cs), which form exclusive interactions with ABA receptors and subfamily 2 Snfl-related kinase (SnRK2s). Here, we report a SnRK2-PP2C complex structure, which reveals marked similarity in PP2C recognition by SnRK2 and ABA receptors. In the complex, the kinase activation loop docks into the active site of PP2C, while the conserved ABA-sensing tryptophan of PP2C inserts into the kinase catalytic cleft, thus mimicking receptor-PP2C interactions. These structural results provide a simple mechanism that directly couples ABA binding to SnRK2 kinase activation and highlight a new paradigm of kinase-phosphatase regulation through mutual packing of their catalytic sites.

引用

页码：85 / 88

页数：4

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