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Title: Molecular Mimicry Regulates ABA Signaling by SnRK2 Kinases and PP2C Phosphatases

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.

Authors:
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  1. (Van Andel)
  2. (
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
FOREIGNNSFOTHERNIH
OSTI Identifier:
1034201
Resource Type:
Journal Article
Resource Relation:
Journal Name: Science; Journal Volume: 335; Journal Issue: 01, 2012
Country of Publication:
United States
Language:
ENGLISH
Subject:
59 BASIC BIOLOGICAL SCIENCES; 60 APPLIED LIFE SCIENCES; 72 PHYSICS OF ELEMENTARY PARTICLES AND FIELDS; ABSCISIC ACID; EXCLUSIVE INTERACTIONS; HORMONES; PHOSPHATASES; PHOSPHOTRANSFERASES; PROTEINS; REGULATIONS; STRESSES; TRYPTOPHAN

Citation Formats

Soon, Fen-Fen, Ng, Ley-Moy, Zhou, X. Edward, West, Graham M., Kovach, Amanda, Tan, M.H. Eileen, Suino-Powell, Kelly M., He, Yuanzheng, Xu, Yong, Chalmers, Michael J., Brunzelle, Joseph S., Zhang, Huiming, Yang, Huaiyu, Jiang, Hualiang, Li, Jun, Yong, Eu-Leong, Cutler, Sean, Zhu, Jian-Kang, Griffin, Patrick R., Melcher, Karsten, Xu, H. Eric, Scripps), NWU), Purdue), UCR), Chinese Aca. Sci.), and NU Singapore). Molecular Mimicry Regulates ABA Signaling by SnRK2 Kinases and PP2C Phosphatases. United States: N. p., 2014. Web. doi:10.1126/science.1215106.
Soon, Fen-Fen, Ng, Ley-Moy, Zhou, X. Edward, West, Graham M., Kovach, Amanda, Tan, M.H. Eileen, Suino-Powell, Kelly M., He, Yuanzheng, Xu, Yong, Chalmers, Michael J., Brunzelle, Joseph S., Zhang, Huiming, Yang, Huaiyu, Jiang, Hualiang, Li, Jun, Yong, Eu-Leong, Cutler, Sean, Zhu, Jian-Kang, Griffin, Patrick R., Melcher, Karsten, Xu, H. Eric, Scripps), NWU), Purdue), UCR), Chinese Aca. Sci.), & NU Singapore). Molecular Mimicry Regulates ABA Signaling by SnRK2 Kinases and PP2C Phosphatases. United States. doi:10.1126/science.1215106.
Soon, Fen-Fen, Ng, Ley-Moy, Zhou, X. Edward, West, Graham M., Kovach, Amanda, Tan, M.H. Eileen, Suino-Powell, Kelly M., He, Yuanzheng, Xu, Yong, Chalmers, Michael J., Brunzelle, Joseph S., Zhang, Huiming, Yang, Huaiyu, Jiang, Hualiang, Li, Jun, Yong, Eu-Leong, Cutler, Sean, Zhu, Jian-Kang, Griffin, Patrick R., Melcher, Karsten, Xu, H. Eric, Scripps), NWU), Purdue), UCR), Chinese Aca. Sci.), and NU Singapore). Thu . "Molecular Mimicry Regulates ABA Signaling by SnRK2 Kinases and PP2C Phosphatases". United States. doi:10.1126/science.1215106.
@article{osti_1034201,
title = {Molecular Mimicry Regulates ABA Signaling by SnRK2 Kinases and PP2C Phosphatases},
author = {Soon, Fen-Fen and Ng, Ley-Moy and Zhou, X. Edward and West, Graham M. and Kovach, Amanda and Tan, M.H. Eileen and Suino-Powell, Kelly M. and He, Yuanzheng and Xu, Yong and Chalmers, Michael J. and Brunzelle, Joseph S. and Zhang, Huiming and Yang, Huaiyu and Jiang, Hualiang and Li, Jun and Yong, Eu-Leong and Cutler, Sean and Zhu, Jian-Kang and Griffin, Patrick R. and Melcher, Karsten and Xu, H. Eric and Scripps) and NWU) and Purdue) and UCR) and Chinese Aca. Sci.) and NU Singapore)},
abstractNote = {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.},
doi = {10.1126/science.1215106},
journal = {Science},
number = 01, 2012,
volume = 335,
place = {United States},
year = {Thu Oct 02 00:00:00 EDT 2014},
month = {Thu Oct 02 00:00:00 EDT 2014}
}