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Architecture and autoinhibitory mechanism of the plasma membrane Na+/H+ antiporter SOS1 in Arabidopsis

Author

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  • Yuhang Wang

    (Chinese Academy of Sciences
    Chinese Academy of Sciences
    University of Chinese Academy of Sciences)

  • Chengcai Pan

    (Guangdong Ocean University)

  • Qihao Chen

    (Chinese Academy of Sciences
    Chinese Academy of Sciences
    University of Chinese Academy of Sciences)

  • Qing Xie

    (Guangdong Ocean University)

  • Yiwei Gao

    (Chinese Academy of Sciences
    Chinese Academy of Sciences
    University of Chinese Academy of Sciences)

  • Lingli He

    (Chinese Academy of Sciences
    Chinese Academy of Sciences
    University of Chinese Academy of Sciences)

  • Yue Li

    (Chinese Academy of Sciences
    Chinese Academy of Sciences
    University of Chinese Academy of Sciences)

  • Yanli Dong

    (Chinese Academy of Sciences
    Chinese Academy of Sciences
    University of Chinese Academy of Sciences)

  • Xingyu Jiang

    (Guangdong Ocean University)

  • Yan Zhao

    (Chinese Academy of Sciences
    Chinese Academy of Sciences
    University of Chinese Academy of Sciences)

Abstract

Salt-overly-sensitive 1 (SOS1) is a unique electroneutral Na+/H+ antiporter at the plasma membrane of higher plants and plays a central role in resisting salt stress. SOS1 is kept in a resting state with basal activity and activated upon phosphorylation. Here, we report the structures of SOS1. SOS1 forms a homodimer, with each monomer composed of transmembrane and intracellular domains. We find that SOS1 is locked in an occluded state by shifting of the lateral-gate TM5b toward the dimerization domain, thus shielding the Na+/H+ binding site. We speculate that the dimerization of the intracellular domain is crucial to stabilize the transporter in this specific conformation. Moreover, two discrete fragments and a residue W1013 are important to prevent the transition of SOS1 to an alternative conformational state, as validated by functional complementation assays. Our study enriches understanding of the alternate access model of eukaryotic Na+/H+ exchangers.

Suggested Citation

  • Yuhang Wang & Chengcai Pan & Qihao Chen & Qing Xie & Yiwei Gao & Lingli He & Yue Li & Yanli Dong & Xingyu Jiang & Yan Zhao, 2023. "Architecture and autoinhibitory mechanism of the plasma membrane Na+/H+ antiporter SOS1 in Arabidopsis," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-40215-y
    DOI: 10.1038/s41467-023-40215-y
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    References listed on IDEAS

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    1. Chiara Lee & Hae Joo Kang & Christoph von Ballmoos & Simon Newstead & Povilas Uzdavinys & David L. Dotson & So Iwata & Oliver Beckstein & Alexander D. Cameron & David Drew, 2013. "A two-domain elevator mechanism for sodium/proton antiport," Nature, Nature, vol. 501(7468), pages 573-577, September.
    2. Yaming Lu & Miao Yu & Yutian Jia & Fan Yang & Yanming Zhang & Xia Xu & Xiaomin Li & Fan Yang & Jianlin Lei & Yi Wang & Guanghui Yang, 2022. "Structural basis for the activity regulation of a potassium channel AKT1 from Arabidopsis," Nature Communications, Nature, vol. 13(1), pages 1-11, December.
    3. Gal Masrati & Manish Dwivedi & Abraham Rimon & Yael Gluck-Margolin & Amit Kessel & Haim Ashkenazy & Itay Mayrose & Etana Padan & Nir Ben-Tal, 2018. "Broad phylogenetic analysis of cation/proton antiporters reveals transport determinants," Nature Communications, Nature, vol. 9(1), pages 1-14, December.
    4. Yanli Dong & Yiwei Gao & Alina Ilie & DuSik Kim & Annie Boucher & Bin Li & Xuejun C. Zhang & John Orlowski & Yan Zhao, 2021. "Structure and mechanism of the human NHE1-CHP1 complex," Nature Communications, Nature, vol. 12(1), pages 1-12, December.
    5. Denisse L. Leyton & Matthew D. Johnson & Rajiv Thapa & Gerard H.M. Huysmans & Rhys A. Dunstan & Nermin Celik & Hsin-Hui Shen & Dorothy Loo & Matthew J. Belousoff & Anthony W. Purcell & Ian R. Henderso, 2014. "A mortise–tenon joint in the transmembrane domain modulates autotransporter assembly into bacterial outer membranes," Nature Communications, Nature, vol. 5(1), pages 1-11, September.
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