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A gate–latch–lock mechanism for hormone signalling by abscisic acid receptors

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  • Karsten Melcher

    (Laboratory of Structural Sciences, Van Andel Research Institute, 333 Bostwick Avenue, N.E., Grand Rapids, Michigan 49503, USA)

  • Ley-Moy Ng

    (Laboratory of Structural Sciences, Van Andel Research Institute, 333 Bostwick Avenue, N.E., Grand Rapids, Michigan 49503, USA
    National University Hospital, Yong Loo Lin School of Medicine, Graduate School for Integrative Sciences & Engineering, National University of Singapore)

  • X. Edward Zhou

    (Laboratory of Structural Sciences, Van Andel Research Institute, 333 Bostwick Avenue, N.E., Grand Rapids, Michigan 49503, USA)

  • Fen-Fen Soon

    (Laboratory of Structural Sciences, Van Andel Research Institute, 333 Bostwick Avenue, N.E., Grand Rapids, Michigan 49503, USA
    National University Hospital, Yong Loo Lin School of Medicine, Graduate School for Integrative Sciences & Engineering, National University of Singapore)

  • Yong Xu

    (Laboratory of Structural Sciences, Van Andel Research Institute, 333 Bostwick Avenue, N.E., Grand Rapids, Michigan 49503, USA)

  • Kelly M. Suino-Powell

    (Laboratory of Structural Sciences, Van Andel Research Institute, 333 Bostwick Avenue, N.E., Grand Rapids, Michigan 49503, USA)

  • Sang-Youl Park

    (University of California at Riverside, Riverside, California 92521, USA)

  • Joshua J. Weiner

    (Medical College of Wisconsin, Milwaukee, Wisconsin 53226, USA)

  • Hiroaki Fujii

    (University of California at Riverside, Riverside, California 92521, USA
    Center for Plant Stress Genomics and Technology, King Abdullah University of Science and Technology)

  • Viswanathan Chinnusamy

    (University of California at Riverside, Riverside, California 92521, USA
    Center for Plant Stress Genomics and Technology, King Abdullah University of Science and Technology)

  • Amanda Kovach

    (Laboratory of Structural Sciences, Van Andel Research Institute, 333 Bostwick Avenue, N.E., Grand Rapids, Michigan 49503, USA)

  • Jun Li

    (Laboratory of Structural Sciences, Van Andel Research Institute, 333 Bostwick Avenue, N.E., Grand Rapids, Michigan 49503, USA
    National University Hospital, Yong Loo Lin School of Medicine, Graduate School for Integrative Sciences & Engineering, National University of Singapore)

  • Yonghong Wang

    (State Key Laboratory of Plant Genomics, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, National Center for Plant Gene Research)

  • Jiayang Li

    (State Key Laboratory of Plant Genomics, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, National Center for Plant Gene Research)

  • Francis C. Peterson

    (Medical College of Wisconsin, Milwaukee, Wisconsin 53226, USA)

  • Davin R. Jensen

    (Medical College of Wisconsin, Milwaukee, Wisconsin 53226, USA)

  • Eu-Leong Yong

    (National University Hospital, Yong Loo Lin School of Medicine, Graduate School for Integrative Sciences & Engineering, National University of Singapore)

  • Brian F. Volkman

    (Medical College of Wisconsin, Milwaukee, Wisconsin 53226, USA)

  • Sean R. Cutler

    (University of California at Riverside, Riverside, California 92521, USA)

  • Jian-Kang Zhu

    (University of California at Riverside, Riverside, California 92521, USA
    Center for Plant Stress Genomics and Technology, King Abdullah University of Science and Technology)

  • H. Eric Xu

    (Laboratory of Structural Sciences, Van Andel Research Institute, 333 Bostwick Avenue, N.E., Grand Rapids, Michigan 49503, USA)

Abstract

Abscisic acid (ABA) is a ubiquitous hormone that regulates plant growth, development and responses to environmental stresses. Its action is mediated by the PYR/PYL/RCAR family of START proteins, but it remains unclear how these receptors bind ABA and, in turn, how hormone binding leads to inhibition of the downstream type 2C protein phosphatase (PP2C) effectors. Here we report crystal structures of apo and ABA-bound receptors as well as a ternary PYL2–ABA–PP2C complex. The apo receptors contain an open ligand-binding pocket flanked by a gate that closes in response to ABA by way of conformational changes in two highly conserved β-loops that serve as a gate and latch. Moreover, ABA-induced closure of the gate creates a surface that enables the receptor to dock into and competitively inhibit the PP2C active site. A conserved tryptophan in the PP2C inserts directly between the gate and latch, which functions to further lock the receptor in a closed conformation. Together, our results identify a conserved gate–latch–lock mechanism underlying ABA signalling.

Suggested Citation

  • Karsten Melcher & Ley-Moy Ng & X. Edward Zhou & Fen-Fen Soon & Yong Xu & Kelly M. Suino-Powell & Sang-Youl Park & Joshua J. Weiner & Hiroaki Fujii & Viswanathan Chinnusamy & Amanda Kovach & Jun Li & Y, 2009. "A gate–latch–lock mechanism for hormone signalling by abscisic acid receptors," Nature, Nature, vol. 462(7273), pages 602-608, December.
  • Handle: RePEc:nat:nature:v:462:y:2009:i:7273:d:10.1038_nature08613
    DOI: 10.1038/nature08613
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    Cited by:

    1. Shen Huang & Chunli Wang & Zixuan Ding & Yaqian Zhao & Jing Dai & Jia Li & Haining Huang & Tongkai Wang & Min Zhu & Mingfeng Feng & Yinghua Ji & Zhongkai Zhang & Xiaorong Tao, 2024. "A plant NLR receptor employs ABA central regulator PP2C-SnRK2 to activate antiviral immunity," Nature Communications, Nature, vol. 15(1), pages 1-14, December.
    2. Zhang You & Shiyuan Guo & Qiao Li & Yanjun Fang & Panpan Huang & Chuanfeng Ju & Cun Wang, 2023. "The CBL1/9-CIPK1 calcium sensor negatively regulates drought stress by phosphorylating the PYLs ABA receptor," Nature Communications, Nature, vol. 14(1), pages 1-14, December.

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