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Structural basis for mechanotransduction in a potassium-dependent mechanosensitive ion channel

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  • Jonathan Mount

    (Washington University School of Medicine
    Washington University School of Medicine)

  • Grigory Maksaev

    (Washington University School of Medicine
    Washington University School of Medicine)

  • Brock T. Summers

    (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)

  • Peng Yuan

    (Washington University School of Medicine
    Washington University School of Medicine)

Abstract

Mechanosensitive channels of small conductance, found in many living organisms, open under elevated membrane tension and thus play crucial roles in biological response to mechanical stress. Amongst these channels, MscK is unique in that its activation also requires external potassium ions. To better understand this dual gating mechanism by force and ligand, we elucidate distinct structures of MscK along the gating cycle using cryo-electron microscopy. The heptameric channel comprises three layers: a cytoplasmic domain, a periplasmic gating ring, and a markedly curved transmembrane domain that flattens and expands upon channel opening, which is accompanied by dilation of the periplasmic ring. Furthermore, our results support a potentially unifying mechanotransduction mechanism in ion channels depicted as flattening and expansion of the transmembrane domain.

Suggested Citation

  • 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.
    • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-34737-0
    DOI: 10.1038/s41467-022-34737-0
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    References listed on IDEAS

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    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. Kirill D. Nadezhdin & Irina A. Talyzina & Aravind Parthasarathy & Arthur Neuberger & David X. Zhang & Alexander I. Sobolevsky, 2023. "Structure of human TRPV4 in complex with GTPase RhoA," Nature Communications, Nature, vol. 14(1), pages 1-11, December.

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