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Structural mechanism for gating of a eukaryotic mechanosensitive channel of small conductance

Author

Listed:
  • Zengqin Deng

    (Washington University School of Medicine
    Center for the Investigation of Membrane Excitability Diseases, Washington University School of Medicine)

  • Grigory Maksaev

    (Washington University School of Medicine
    Center for the Investigation of Membrane Excitability Diseases, Washington University School of Medicine)

  • Angela M. Schlegel

    (Washington University in Saint Louis
    NSF Center for Engineering Mechanobiology, Washington University in Saint Louis)

  • Jingying Zhang

    (Washington University School of Medicine
    Center for the Investigation of Membrane Excitability Diseases, Washington University School of Medicine)

  • Michael Rau

    (Washington University Center for Cellular Imaging, Washington University School of Medicine)

  • James A. J. Fitzpatrick

    (Washington University School of Medicine
    Washington University Center for Cellular Imaging, Washington University School of Medicine
    Washington University School of Medicine
    Washington University in Saint Louis)

  • Elizabeth S. Haswell

    (Washington University in Saint Louis
    NSF Center for Engineering Mechanobiology, Washington University in Saint Louis)

  • Peng Yuan

    (Washington University School of Medicine
    Center for the Investigation of Membrane Excitability Diseases, Washington University School of Medicine)

Abstract

Mechanosensitive ion channels transduce physical force into electrochemical signaling that underlies an array of fundamental physiological processes, including hearing, touch, proprioception, osmoregulation, and morphogenesis. The mechanosensitive channels of small conductance (MscS) constitute a remarkably diverse superfamily of channels critical for management of osmotic pressure. Here, we present cryo-electron microscopy structures of a MscS homolog from Arabidopsis thaliana, MSL1, presumably in both the closed and open states. The heptameric MSL1 channel contains an unusual bowl-shaped transmembrane region, which is reminiscent of the evolutionarily and architecturally unrelated mechanosensitive Piezo channels. Upon channel opening, the curved transmembrane domain of MSL1 flattens and expands. Our structures, in combination with functional analyses, delineate a structural mechanism by which mechanosensitive channels open under increased membrane tension. Further, the shared structural feature between unrelated channels suggests the possibility of a unified mechanical gating mechanism stemming from membrane deformation induced by a non-planar transmembrane domain.

Suggested Citation

  • Zengqin Deng & Grigory Maksaev & Angela M. Schlegel & Jingying Zhang & Michael Rau & James A. J. Fitzpatrick & Elizabeth S. Haswell & Peng Yuan, 2020. "Structural mechanism for gating of a eukaryotic mechanosensitive channel of small conductance," Nature Communications, Nature, vol. 11(1), pages 1-9, December.
  • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-17538-1
    DOI: 10.1038/s41467-020-17538-1
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    Cited by:

    1. Jingying Zhang & Grigory Maksaev & Peng Yuan, 2023. "Open structure and gating of the Arabidopsis mechanosensitive ion channel MSL10," Nature Communications, Nature, vol. 14(1), pages 1-9, December.
    2. Jonathan Mount & Grigory Maksaev & Brock T. Summers & James A. J. Fitzpatrick & Peng Yuan, 2022. "Structural basis for mechanotransduction in a potassium-dependent mechanosensitive ion channel," Nature Communications, Nature, vol. 13(1), pages 1-11, December.
    3. Sebastian Jojoa-Cruz & Kei Saotome & Che Chun Alex Tsui & Wen-Hsin Lee & Mark S. P. Sansom & Swetha E. Murthy & Ardem Patapoutian & Andrew B. Ward, 2022. "Structural insights into the Venus flytrap mechanosensitive ion channel Flycatcher1," Nature Communications, Nature, vol. 13(1), pages 1-11, December.
    4. Zhihui He & Yonghui Zhao & Michael J. Rau & James A. J. Fitzpatrick & Rajan Sah & Hongzhen Hu & Peng Yuan, 2023. "Structural and functional analysis of human pannexin 2 channel," Nature Communications, Nature, vol. 14(1), pages 1-10, December.
    5. Ruo-Xu Gu & Bert L. Groot, 2023. "Central cavity dehydration as a gating mechanism of potassium channels," Nature Communications, Nature, vol. 14(1), pages 1-12, December.

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