Visualization of the mechanosensitive ion channel MscS under membrane tension

Yixiao Zhang, Csaba Daday, Ruo-Xu Gu, Charles D. Cox, Boris Martinac, Bert L. Groot and Thomas Walz ()
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Yixiao Zhang: The Rockefeller University
Csaba Daday: Max Planck Institute for Biophysical Chemistry
Ruo-Xu Gu: Max Planck Institute for Biophysical Chemistry
Charles D. Cox: University of New South Wales
Boris Martinac: University of New South Wales
Bert L. Groot: Max Planck Institute for Biophysical Chemistry
Thomas Walz: The Rockefeller University

Nature, 2021, vol. 590, issue 7846, 509-514

Abstract: Abstract Mechanosensitive channels sense mechanical forces in cell membranes and underlie many biological sensing processes1–3. However, how exactly they sense mechanical force remains under investigation4. The bacterial mechanosensitive channel of small conductance, MscS, is one of the most extensively studied mechanosensitive channels4–8, but how it is regulated by membrane tension remains unclear, even though the structures are known for its open and closed states9–11. Here we used cryo-electron microscopy to determine the structure of MscS in different membrane environments, including one that mimics a membrane under tension. We present the structures of MscS in the subconducting and desensitized states, and demonstrate that the conformation of MscS in a lipid bilayer in the open state is dynamic. Several associated lipids have distinct roles in MscS mechanosensation. Pore lipids are necessary to prevent ion conduction in the closed state. Gatekeeper lipids stabilize the closed conformation and dissociate with membrane tension, allowing the channel to open. Pocket lipids in a solvent-exposed pocket between subunits are pulled out under sustained tension, allowing the channel to transition to the subconducting state and then to the desensitized state. Our results provide a mechanistic underpinning and expand on the ‘force-from-lipids’ model for MscS mechanosensation4,11.

Date: 2021
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DOI: 10.1038/s41586-021-03196-w

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