Author's School

Arts & Sciences

Author's Department

Biology

Document Type

Article

Publication Date

7-23-2020

Originally Published In

Deng Z, Maksaev G, Schlegel AM, Zhang J, Rau M, Fitzpatrick JAJ, Haswell ES, Yuan P. Structural mechanism for gating of a eukaryotic mechanosensitive channel of small conductance. Nat Commun. 2020 Jul 23;11(1):3690. doi: 10.1038/s41467-020-17538-1. PMID: 32704140; PMCID: PMC7378837.

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.

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Supplementary information is available for this paper at https://doi.org/10.1038/s41467-020-17538-1.

Creative Commons License

Creative Commons Attribution 4.0 International License
This work is licensed under a Creative Commons Attribution 4.0 International License.

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