Evidence map›Paper›PMID 36715097›Full record

ArticleeLife2023

State-specific morphological deformations of the lipid bilayer explain mechanosensitive gating of MscS ion channels.

Yein Christina Park, Bharat Reddy, Navid Bavi, Eduardo Perozo, José D Faraldo-Gómez

Open access · goldAbstract read
In one paragraph

Article in eLife, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
3.4field-weighted citation impact, top 7% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

15 citing papers in PubMed, 23 citations in OpenAlex.

  1. Review
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  6. Models of Cellular Mechanosensation.Results and problems in cell differentiation · 2026
    Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

Yein Christina ParkTheoretical Molecular Biophysics Laboratory, National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, United States.ORCID 0000-0002-5011-7421
Bharat ReddyDepartment of Biochemistry and Molecular Biology, University of Chicago, Chicago, United States.
Navid BaviDepartment of Biochemistry and Molecular Biology, University of Chicago, Chicago, United States.
Eduardo PerozoDepartment of Biochemistry and Molecular Biology, University of Chicago, Chicago, United States.ORCID 0000-0001-7132-2793
José D Faraldo-GómezTheoretical Molecular Biophysics Laboratory, National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, United States.ORCID 0000-0001-7224-7676
University of Chicago · USNational Institutes of Health · US

Funding

Molecular Mechanisms in Membrane Bioenergetics, Transport and SignalingZIAHL006203 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI FARALDO-GÓMEZ, JOSE · 2015 to 2023
$15.4M
Breakthrough Molecular Dynamics Research via an Anton2 SupercomputerR01GM116961 · NIGMS · CARNEGIE-MELLON UNIVERSITY · PI BLOOD, PHILIP D. · 2016 to 2023
$3.0M
NIGMS NIH HHS R01 GM116961NIH HHS IRPNIH HHS R01GM131191
6 · The paper itself

Abstract

The force-from-lipids hypothesis of cellular mechanosensation posits that membrane channels open and close in response to changes in the physical state of the lipid bilayer, induced for example by lateral tension. Here, we investigate the molecular basis for this transduction mechanism by studying the mechanosensitive ion channel MscS from Escherichia coli and its eukaryotic homolog MSL1 from Arabidopsis thaliana. First, we use single-particle cryo-electron microscopy to determine the structure of a novel open conformation of wild-type MscS, stabilized in a thinned lipid nanodisc. Compared with the closed state, the structure shows a reconfiguration of helices TM1, TM2, and TM3a, and widening of the central pore. Based on these structures, we examined how the morphology of the membrane is altered upon gating, using molecular dynamics simulations. The simulations reveal that closed-state MscS causes drastic protrusions in the inner leaflet of the lipid bilayer, both in the absence and presence of lateral tension, and for different lipid compositions. These deformations arise to provide adequate solvation to hydrophobic crevices under the TM1-TM2 hairpin, and clearly reflect a high-energy conformation for the membrane, particularly under tension. Strikingly, these protrusions are largely eradicated upon channel opening. An analogous computational study of open and closed MSL1 recapitulates these findings. The gating equilibrium of MscS channels thus appears to be dictated by opposing conformational preferences, namely those of the lipid membrane and of the protein structure. We propose a membrane deformation model of mechanosensation, which posits that tension shifts the gating equilibrium towards the conductive state not because it alters the mode in which channel and lipids interact, but because it increases the energetic cost of the morphological perturbations in the membrane required by the closed state.

Indexed as

Escherichia coliEscherichia coli ProteinsLipid BilayersCryoelectron MicroscopyIon ChannelsMechanotransduction, CellularMolecular Dynamics SimulationEscherichia coli ProteinsIon ChannelsLipid BilayersMscS protein, E colicryo-electron microscopyE. coliion channelsmechanosensationmembrane morphologymolecular biophysicsmolecular dynamics simulationstructural biology

Identifiers

PMID36715097
PMCPMC9925053
OpenAlexW4318478190

What OpenQuestion holds

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LicenceCC0
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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.