Evidence map›Paper›PMID 40796571›Full record

ArticleNature communications2025

Lipid interactions and gating hysteresis suggest a physiological role for mechanosensitive channel YnaI.

Nathan Will, Giorgos Hiotis, Yoshitaka Nakayama, Gabriella Angiulli, Zijing Zhou, Charles D Cox, Boris Martinac, Thomas Walz

Abstract read
In one paragraph

Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
–field-weighted citation impact
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

6 citing papers in PubMed.

  1. Review
  2. The MscS channel frombioRxiv : the preprint server for biology · 2026
    Article
  3. Article
  4. Hysteretic Conductance in Ion Channel Gating.Entropy (Basel, Switzerland) · 2026
    Review
  5. Review
  6. Article
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

8 authors.

Nathan Will *Laboratory of Molecular Electron Microscopy, The Rockefeller University, New York, NY, USA.ORCID http://orcid.org/0000-0002-9373-5334
Giorgos Hiotis *Laboratory of Molecular Electron Microscopy, The Rockefeller University, New York, NY, USA.
Yoshitaka Nakayama *Laboratory of Molecular Electron Microscopy, The Rockefeller University, New York, NY, USA.ORCID http://orcid.org/0000-0001-6797-5556
Gabriella AngiulliLaboratory of Molecular Electron Microscopy, The Rockefeller University, New York, NY, USA.
Zijing ZhouSt Vincent's Clinical School, University of New South Wales, Sydney, NSW, Australia.
Charles D CoxSt Vincent's Clinical School, University of New South Wales, Sydney, NSW, Australia.ORCID http://orcid.org/0000-0002-3802-6746
Boris MartinacSt Vincent's Clinical School, University of New South Wales, Sydney, NSW, Australia.ORCID http://orcid.org/0000-0001-8422-7082
Thomas WalzLaboratory of Molecular Electron Microscopy, The Rockefeller University, New York, NY, USA. twalz@rockefeller.edu.ORCID http://orcid.org/0000-0003-2606-2835

Funding

Elucidating the gating mechanisms of bacterial mechanosensitive channelsR01GM144581 · NIGMS · ROCKEFELLER UNIVERSITY · PI THOMAS WALZ · 2023 to 2026
$2.0M
NIGMS NIH HHS R01 GM144581
6 · The paper itself

Abstract

YnaI is a member of the family of bacterial MscS (mechanosensitive channel of small conductance)-like channels. Channel gating upon hypoosmotic stress and the role of lipids in this process have been extensively studied for MscS, but are less well understood for YnaI, which features two additional transmembrane helices. Here, we combined cryogenic electron microscopy, molecular dynamics simulations and patch-clamp electrophysiology to advance our understanding of YnaI. The two additional helices move the lipid-filled hydrophobic pockets in YnaI further away from the lipid bilayer and change the function of the pocket lipids from being a critical gating element in MscS to being more of a structural element in YnaI. Unlike MscS, YnaI shows pronounced gating hysteresis and remains open to a substantially lower membrane tension than is needed to initially open the channel. Thus, at near-lytic membrane tension, both MscL and YnaI will open, but while MscL has a large pore and must close quickly to minimize loss of essential metabolites, YnaI only conducts ions and can thus remain open for longer to continue to facilitate pressure equilibration across the membrane.

Indexed as

Escherichia coli ProteinsIon Channel GatingIon ChannelsCell MembraneCryoelectron MicroscopyEscherichia coliHydrophobic and Hydrophilic InteractionsLipid BilayersMechanotransduction, CellularMolecular Dynamics SimulationPatch-Clamp TechniquesEscherichia coli ProteinsIon ChannelsLipid BilayersMscL protein, E coliMscS protein, E coli

Identifiers

PMID40796571
PMCPMC12344017

What OpenQuestion holds

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LicenceCC BY-NC-ND
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Registered trials

None linked

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.