Evidence map›Paper›PMID 37805510›Full record

ArticleNature communications2023

Open structure and gating of the Arabidopsis mechanosensitive ion channel MSL10.

Jingying Zhang, Grigory Maksaev, Peng Yuan

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

10 citing papers in PubMed, 10 citations in OpenAlex.

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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

3 authors at 1 institution in 1 country.

Jingying ZhangDepartment of Cell Biology and Physiology, Washington University School of Medicine, Saint Louis, MO, USA.
Grigory MaksaevDepartment of Cell Biology and Physiology, Washington University School of Medicine, Saint Louis, MO, USA.ORCID 0000-0001-6242-1634
Peng YuanDepartment of Cell Biology and Physiology, Washington University School of Medicine, Saint Louis, MO, USA. peng.yuan@mssm.edu.ORCID 0000-0002-5660-225X
Washington University in St. Louis · US

Funding

Structural Mechanism for Gating of Mechanosensitive ChannelsR01GM143440 · NIGMS · WASHINGTON UNIVERSITY · PI YUAN, PENG · 2022 to 2025
$1.6M
NIGMS NIH HHS R01 GM143440
6 · The paper itself

Abstract

Plants are challenged by drastically different osmotic environments during growth and development. Adaptation to these environments often involves mechanosensitive ion channels that can detect and respond to mechanical force. In the model plant Arabidopsis thaliana, the mechanosensitive channel MSL10 plays a crucial role in hypo-osmotic shock adaptation and programmed cell death induction, but the molecular basis of channel function remains poorly understood. Here, we report a structural and electrophysiological analysis of MSL10. The cryo-electron microscopy structures reveal a distinct heptameric channel assembly. Structures of the wild-type channel in detergent and lipid environments, and in the absence of membrane tension, capture an open conformation. Furthermore, structural analysis of a non-conductive mutant channel demonstrates that reorientation of phenylalanine side chains alone, without main chain rearrangements, may generate the hydrophobic gate. Together, these results reveal a distinct gating mechanism and advance our understanding of mechanotransduction.

Indexed as

ArabidopsisArabidopsis ProteinsCryoelectron MicroscopyIon ChannelsMechanotransduction, CellularMembrane ProteinsArabidopsis ProteinsIon ChannelsMembrane ProteinsMSL10 protein, Arabidopsis

Identifiers

PMID37805510
PMCPMC10560256
OpenAlexW4387424349

What OpenQuestion holds

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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.