Evidence map›Paper›PMID 31090543›Full record

ArticleeLife2019

Symmetry transitions during gating of the TRPV2 ion channel in lipid membranes.

Lejla Zubcevic, Allen L Hsu, Mario J Borgnia, Seok-Yong Lee

Open access · goldAbstract read
In one paragraph

Article in eLife, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
4.9field-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

29 citing papers in PubMed, 43 citations in OpenAlex.

  1. An Extracellular Pore‑Targeting Peptide Defines a Designable Allosteric Site in TRPV2.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  2. Symmetry-driven gating of TRPM8 by PIPNature communications · 2026
    Article
  3. Article
  4. Structural Pharmacology of TRPV4 Antagonists.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Article
  5. Article
  6. Article
  7. Membrane protein isolation and structure determination in cell-derived membrane vesicles.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  8. Article
  9. Sensory TRP Channels in Three Dimensions.Annual review of biochemistry · 2022
    Review
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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

4 authors at 2 institutions in 1 country.

Lejla ZubcevicDepartment of Biochemistry, Duke University School of Medicine, Durham, United States.ORCID 0000-0002-1884-9235
Allen L HsuGenome Integrity and Structural Biology Laboratory, National Institute of Environmental Health Sciences, National Institutes of Health, Department of Health and Human Services, Research Triangle Park, United States.ORCID 0000-0003-2065-3802
Mario J BorgniaDepartment of Biochemistry, Duke University School of Medicine, Durham, United States.ORCID 0000-0001-9159-1413
Seok-Yong LeeDepartment of Biochemistry, Duke University School of Medicine, Durham, United States.ORCID 0000-0002-0662-9921
Duke University · USNational Institutes of Health · US

Funding

NIEHS Cryo-EM Core FacilityZICES103326 · NIEHS · NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES · PI BORGNIA, MARIO · 2017 to 2025
$17.0M
Structure, function, and pharmacology of neuronal membrane transport proteinsR35NS097241 · NINDS · DUKE UNIVERSITY · PI LEE, SEOK-YONG · 2016 to 2023
$6.1M
Intramural NIH HHS ZIC ES103326NIEHS NIH HHS ZIC ES103326NINDS NIH HHS R35 NS097241NINDS NIH HHS R35NS097241
6 · The paper itself

Abstract

The Transient Receptor Potential Vanilloid 2 (TRPV2) channel is a member of the temperature-sensing thermoTRPV family. Recent advances in cryo-electronmicroscopy (cryo-EM) and X-ray crystallography have provided many important insights into the gating mechanisms of thermoTRPV channels. Interestingly, crystallographic studies of ligand-dependent TRPV2 gating have shown that the TRPV2 channel adopts two-fold symmetric arrangements during the gating cycle. However, it was unclear if crystal packing forces played a role in stabilizing the two-fold symmetric arrangement of the channel. Here, we employ cryo-EM to elucidate the structure of full-length rabbit TRPV2 in complex with the agonist resiniferatoxin (RTx) in nanodiscs and amphipol. We show that RTx induces two-fold symmetric conformations of TRPV2 in both environments. However, the two-fold symmetry is more pronounced in the native-like lipid environment of the nanodiscs. Our data offers insights into a gating pathway in TRPV2 involving symmetry transitions.

Indexed as

AnimalsCryoelectron MicroscopyDiterpenesMembranesProtein BindingProtein ConformationRabbitsTRPV Cation ChannelsDiterpenesresiniferatoxinTRPV Cation ChannelsCa2+ permeable channelcryo-EMheat sensing ion channelligand gated ion channelmolecular biophysicsOryctolagus cuniculusstructural biologyTRP channel

Identifiers

PMID31090543
PMCPMC6544438
OpenAlexW2911734155

What OpenQuestion holds

Textmetadata
LicenceCC0
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.