Evidence map›Paper›PMID 32704140›Full record

ArticleNature communications2020

Structural mechanism for gating of a eukaryotic mechanosensitive channel of small conductance.

Zengqin Deng, Grigory Maksaev, Angela M Schlegel, Jingying Zhang, Michael Rau, James A J Fitzpatrick, Elizabeth S Haswell, Peng Yuan

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
5.3field-weighted citation impact, top 3% 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

30 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
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  5. Electronic Polarizability Tunes the Function of the Human Bestrophin 1 ClJournal of chemical theory and computation · 2025
    Article
  6. Electronic Polarizability Tunes the Function of the Human Bestrophin 1 ClbioRxiv : the preprint server for biology · 2024
    Article
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  18. Article
  19. Physics of mechanotransduction by Piezo ion channels.The Journal of general physiology · 2022
    Review
  20. 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 at 1 institution in 1 country.

Zengqin DengDepartment of Cell Biology and Physiology, Washington University School of Medicine, Saint Louis, MO, 63110, USA.ORCID http://orcid.org/0000-0002-5658-2068
Grigory Maksaev *Department of Cell Biology and Physiology, Washington University School of Medicine, Saint Louis, MO, 63110, USA.ORCID http://orcid.org/0000-0001-6242-1634
Angela M Schlegel *Department of Biology, Washington University in Saint Louis, Saint Louis, MO, 63130, USA.ORCID http://orcid.org/0000-0001-5253-5769
Jingying ZhangDepartment of Cell Biology and Physiology, Washington University School of Medicine, Saint Louis, MO, 63110, USA.
Michael RauWashington University Center for Cellular Imaging, Washington University School of Medicine, Saint Louis, MO, 63110, USA.ORCID http://orcid.org/0000-0001-5170-2000
James A J FitzpatrickDepartment of Cell Biology and Physiology, Washington University School of Medicine, Saint Louis, MO, 63110, USA.ORCID http://orcid.org/0000-0002-7907-3602
Elizabeth S HaswellDepartment of Biology, Washington University in Saint Louis, Saint Louis, MO, 63130, USA.ORCID http://orcid.org/0000-0002-4246-065X
Peng YuanDepartment of Cell Biology and Physiology, Washington University School of Medicine, Saint Louis, MO, 63110, USA. yuanp@wustl.edu.ORCID http://orcid.org/0000-0002-5660-225X
Washington University in St. Louis · US

Funding

Howard Hughes Medical Institute
6 · The paper itself

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.

Indexed as

Ion Channel GatingMechanotransduction, CellularArabidopsisArabidopsis ProteinsEscherichia coli ProteinsEukaryotaIon ChannelsModels, MolecularMutant ProteinsProtein DomainsProtein Structure, SecondaryArabidopsis ProteinsAT4G00290 protein, ArabidopsisEscherichia coli ProteinsIon ChannelsMscS protein, E coliMutant Proteins

Identifiers

PMID32704140
PMCPMC7378837
OpenAlexW3044636025

What OpenQuestion holds

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LicenceCC BY
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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.