Evidence map›Paper›PMID 36371466›Full record

ArticleNature communications2022

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

Jonathan Mount, Grigory Maksaev, Brock T Summers, James A J Fitzpatrick, Peng Yuan

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

17 citing papers in PubMed, 18 citations in OpenAlex.

  1. Review
  2. The MscS channel frombioRxiv : the preprint server for biology · 2026
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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 1 institution in 1 country.

Jonathan MountDepartment of Cell Biology and Physiology, Washington University School of Medicine, Saint Louis, MO, USA.ORCID 0000-0001-5366-0449
Grigory MaksaevDepartment of Cell Biology and Physiology, Washington University School of Medicine, Saint Louis, MO, USA.ORCID 0000-0001-6242-1634
Brock T SummersWashington University Center for Cellular Imaging, Washington University School of Medicine, Saint Louis, MO, USA.
James A J FitzpatrickDepartment of Cell Biology and Physiology, Washington University School of Medicine, Saint Louis, MO, USA.ORCID 0000-0002-7907-3602
Peng YuanDepartment of Cell Biology and Physiology, Washington University School of Medicine, Saint Louis, MO, USA. yuanp@wustl.edu.ORCID 0000-0002-5660-225X
Washington University in St. Louis · US

Funding

Washington University Center for Cellular ImagingP30CA091842 · NCI · WASHINGTON UNIVERSITY · PI AIMEE S JAMES · 2001 to 2026
$128.0M
STRUCTURE AND MECHANISM OF A POLYMODAL TRP ION CHANNELR01NS099341 · NINDS · WASHINGTON UNIVERSITY · PI YUAN, PENG · 2017 to 2021
$1.7M
Structural Mechanism for Gating of Mechanosensitive ChannelsR01GM143440 · NIGMS · WASHINGTON UNIVERSITY · PI YUAN, PENG · 2022 to 2025
$1.6M
NCI NIH HHS P30 CA091842NIGMS NIH HHS R01 GM143440NINDS NIH HHS R01 NS099341
6 · The paper itself

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.

Indexed as

Ion Channel GatingPotassium ChannelsCryoelectron MicroscopyIon ChannelsMechanotransduction, CellularModels, MolecularPotassiumIon ChannelsPotassiumPotassium Channels

Identifiers

PMID36371466
PMCPMC9653487
OpenAlexW4309046853

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

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.