Molecular Mimicry Regulates ABA Signaling by SnRK2 Kinases and PP2C Phosphatases

Overview

Journal Science

Specialty Science

Date 2011 Nov 26

PMID 22116026

Citations 231

Authors

Fen-Fen Soon

Ley-Moy Ng

X Edward Zhou

Graham M West

Amanda Kovach

M H Eileen Tan

Kelly M Suino-Powell

Yuanzheng He

Yong Xu

Michael J Chalmers

Joseph S Brunzelle

Huiming Zhang

Huaiyu Yang

Hualiang Jiang

Jun Li

Eu-Leong Yong

Sean Cutler

Jian-Kang Zhu

Patrick R Griffin

Karsten Melcher

H Eric Xu

Affiliations

Soon will be listed here.

Abstract

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.

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