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

Jonathan Mount, Grigory Maksaev, Brock T. Summers, James A. J. Fitzpatrick and Peng Yuan ()
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Jonathan Mount: Washington University School of Medicine
Grigory Maksaev: 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
Peng Yuan: Washington University School of Medicine

Nature Communications, 2022, vol. 13, issue 1, 1-11

Abstract: 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.

Date: 2022
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DOI: 10.1038/s41467-022-34737-0

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