Evidence map›Paper›PMID 40374654›Full record

ArticleNature communications2025

Structural dynamics and permeability of the TRPV3 pentamer.

Shifra Lansky, Zhaokun Wang, Oliver B Clarke, Christophe Chipot, Simon Scheuring

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 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. Symmetry-driven gating of TRPM8 by PIPNature communications · 2026
    Article
  5. Biomolecular assemblies through weak noncovalent interactions: Higher-order transient structures and their condensate phase.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  6. Article
  7. 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

5 authors.

Shifra LanskyDepartment of Anesthesiology, Weill Cornell Medicine, New York, NY, USA.
Zhaokun WangDepartment of Anesthesiology, Weill Cornell Medicine, New York, NY, USA.
Oliver B ClarkeDepartment of Anesthesiology, Columbia University Irving Medical Center, New York, NY, USA.ORCID http://orcid.org/0000-0003-1876-196X
Christophe ChipotLaboratoire International Associé CNRS and University of Illinois at Urbana-Champaign, Université de Lorraine, Vandœuvre-lès-Nancy, France.
Simon ScheuringDepartment of Anesthesiology, Weill Cornell Medicine, New York, NY, USA. sis2019@med.cornell.edu.ORCID http://orcid.org/0000-0003-3534-069X

Funding

Enabling physical stimuli in the study of structural dynamics: The sensory ion channelsDP1AT010874 · NCCIH · WEILL MEDICAL COLL OF CORNELL UNIV · PI SCHEURING, SIMON · 2019 to 2023
$5.9M
Structure and Function of a Pentameric TRPV3 ChannelR01NS134559 · NINDS · WEILL MEDICAL COLL OF CORNELL UNIV · PI Simon Scheuring · 2024 to 2026
$1.8M
NINDS NIH HHS R01 NS134559U.S. Department of Health & Human Services | NIH | National Center for Complementary and Integrative Health (NCCIH) DP1AT010874U.S. Department of Health & Human Services | NIH | National Institute of Neurological Disorders and Stroke (NINDS) R01NS134559
6 · The paper itself

Abstract

TRPV3 belongs to the large superfamily of tetrameric transient receptor potential (TRP) ion channels. Recently, using high-speed atomic force microscopy (HS-AFM), we discovered a rare and transient pentameric state for TRPV3 that is in equilibrium with the tetrameric state, and, using cryo-EM, we solved a low-resolution structure of the TRPV3 pentamer, in which, however, many residues were unresolved. Here, we present a higher resolution and more complete structure of the pentamer, revealing a domain-swapped architecture, a collapsed vanilloid binding site, and a large pore. Molecular dynamics simulations and potential of mean force calculations of the pentamer establish high protein dynamics and permeability to large cations. Subunit interface analysis, together with thermal denaturation experiments, led us to propose a molecular mechanism of the tetramer-to-pentamer transition, backed experimentally by HS-AFM observations. Collectively, our data demonstrate that the TRPV3 pentamer is in a hyper-activated state with unique, highly permissive permeation properties.

Indexed as

TRPV Cation ChannelsAnimalsBinding SitesCryoelectron MicroscopyHumansMicroscopy, Atomic ForceMolecular Dynamics SimulationPermeabilityProtein MultimerizationTRPV3 protein, humanTRPV Cation Channels

Identifiers

PMID40374654
PMCPMC12081643

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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.