Evidence map›Paper›PMID 35165281›Full record

ArticleNature communications2022

Structural insights into the Venus flytrap mechanosensitive ion channel Flycatcher1.

Sebastian Jojoa-Cruz, Kei Saotome, Che Chun Alex Tsui, Wen-Hsin Lee, Mark S P Sansom, Swetha E Murthy, Ardem Patapoutian, Andrew B Ward

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 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
6.3field-weighted citation impact, top 4% 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

25 citing papers in PubMed, 30 citations in OpenAlex.

  1. The MscS channel frombioRxiv : the preprint server for biology · 2026
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  5. The Nanodisc System for Investigating Protein-Lipid Interactions.Methods in molecular biology (Clifton, N.J.) · 2026
    Review
  6. Asymmetric gating of a homopentameric ion channel GLIC revealed by cryo-EM.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Article
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  10. Article
  11. Article
  12. Electronic Polarizability Tunes the Function of the Human Bestrophin 1 ClJournal of chemical theory and computation · 2025
    Article
  13. Article
  14. Electronic Polarizability Tunes the Function of the Human Bestrophin 1 ClbioRxiv : the preprint server for biology · 2024
    Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
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 4 institutions in 2 countries.

Sebastian Jojoa-Cruz *Department of Integrative Structural and Computational Biology, Scripps Research, La Jolla, CA, 92037, USA.ORCID http://orcid.org/0000-0002-4392-3898
Kei Saotome *Department of Integrative Structural and Computational Biology, Scripps Research, La Jolla, CA, 92037, USA.ORCID http://orcid.org/0000-0002-4135-5356
Che Chun Alex TsuiDepartment of Integrative Structural and Computational Biology, Scripps Research, La Jolla, CA, 92037, USA.ORCID http://orcid.org/0000-0003-4886-9824
Wen-Hsin LeeDepartment of Integrative Structural and Computational Biology, Scripps Research, La Jolla, CA, 92037, USA.ORCID http://orcid.org/0000-0001-9445-6671
Mark S P SansomDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK.ORCID http://orcid.org/0000-0001-6360-7959
Swetha E MurthyHoward Hughes Medical Institute, Department of Neuroscience, Dorris Neuroscience Center, Scripps Research, La Jolla, CA, 92037, USA. murthysw@ohsu.edu.ORCID http://orcid.org/0000-0001-9580-3380
Ardem PatapoutianHoward Hughes Medical Institute, Department of Neuroscience, Dorris Neuroscience Center, Scripps Research, La Jolla, CA, 92037, USA. ardem@scripps.edu.ORCID http://orcid.org/0000-0003-0726-7034
Andrew B WardDepartment of Integrative Structural and Computational Biology, Scripps Research, La Jolla, CA, 92037, USA. andrew@scripps.edu.ORCID http://orcid.org/0000-0001-7153-3769
Scripps Institution of Oceanography · USHoward Hughes Medical Institute · USScripps Research Institute · USUniversity of Oxford · GB

Funding

Resource for Biocomputing Visualization and InformaticsP41GM103311 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FERRIN, THOMAS E · 2012 to 2017
$8.2M
ChimeraX -- Next Generation Visualization and Analysis Software for Multiscale ModelingR01GM129325 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FERRIN, THOMAS E · 2018 to 2025
$5.2M
Molecular understanding of membrane sensorsR01HL143297 · NHLBI · SCRIPPS RESEARCH INSTITUTE, THE · PI PATAPOUTIAN, ARDEM, WARD, ANDREW BARRETT · 2019 to 2022
$3.2M
Biotechnology and Biological Sciences Research Council BB/N000145/1Biotechnology and Biological Sciences Research Council BB/R00126X/1Howard Hughes Medical InstituteNHLBI NIH HHS R01 HL143297NIGMS NIH HHS P41 GM103311NIGMS NIH HHS R01 GM129325Wellcome TrustWellcome Trust (Wellcome) 208361/Z/17/Z
6 · The paper itself

Abstract

Flycatcher1 (FLYC1), a MscS homolog, has recently been identified as a candidate mechanosensitive (MS) ion channel involved in Venus flytrap prey recognition. FLYC1 is a larger protein and its sequence diverges from previously studied MscS homologs, suggesting it has unique structural features that contribute to its function. Here, we characterize FLYC1 by cryo-electron microscopy, molecular dynamics simulations, and electrophysiology. Akin to bacterial MscS and plant MSL1 channels, we find that FLYC1 central core includes side portals in the cytoplasmic cage that regulate ion preference and conduction, by identifying critical residues that modulate channel conductance. Topologically unique cytoplasmic flanking regions can adopt 'up' or 'down' conformations, making the channel asymmetric. Disruption of an up conformation-specific interaction severely delays channel deactivation by 40-fold likely due to stabilization of the channel open state. Our results illustrate novel structural features and likely conformational transitions that regulate mechano-gating of FLYC1.

Indexed as

Cell LineCryoelectron MicroscopyDroseraceaeHEK293 CellsHumansIon Channel GatingIon ChannelsIon TransportMechanotransduction, CellularMolecular Dynamics SimulationPatch-Clamp TechniquesPlant ProteinsProtein ConformationIon ChannelsPlant Proteins

Identifiers

PMID35165281
PMCPMC8844309
OpenAlexW4221109990

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.