Evidence map›Paper›PMID 31070581›Full record

ArticleeLife2019

Regulatory switch at the cytoplasmic interface controls TRPV channel gating.

Lejla Zubcevic, William F Borschel, 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 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
5.5field-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

50 citing papers in PubMed, 73 citations in OpenAlex.

  1. Article
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  4. Review
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  7. Structural insights into TRPV2 modulation by probenecid.Nature structural & molecular biology · 2025
    Article
  8. Article
  9. Article
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  11. Advances in the pathogenesis of rosacea.Frontiers in immunology · 2025
    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

5 authors at 2 institutions in 1 country.

Lejla Zubcevic *Department of Biochemistry, Duke University School of Medicine, Durham, United States.ORCID 0000-0002-1884-9235
William F Borschel *Department of Biochemistry, Duke University School of Medicine, Durham, United States.ORCID 0000-0003-4064-9026
Allen L HsuGenome Integrity and Structural Biology Laboratory, Department of Health and Human Services, National Institute of Environmental Health Sciences, National Institutes of Health, Durham, 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 ES103326NIH HHS Intramural Research ProgramNINDS NIH HHS R35 NS097241NINDS NIH HHS R35NS097241
6 · The paper itself

Abstract

Temperature-sensitive transient receptor potential vanilloid (thermoTRPV) channels are activated by ligands and heat, and are involved in various physiological processes. ThermoTRPV channels possess a large cytoplasmic ring consisting of N-terminal ankyrin repeat domains (ARD) and C-terminal domains (CTD). The cytoplasmic inter-protomer interface is unique and consists of a CTD coiled around a β-sheet which makes contacts with the neighboring ARD. Despite much existing evidence that the cytoplasmic ring is important for thermoTRPV function, the mechanism by which this unique structure is involved in thermoTRPV gating has not been clear. Here, we present cryo-EM and electrophysiological studies which demonstrate that TRPV3 gating involves large rearrangements at the cytoplasmic inter-protomer interface and that this motion triggers coupling between cytoplasmic and transmembrane domains, priming the channel for opening. Furthermore, our studies unveil the role of this interface in the distinct biophysical and physiological properties of individual thermoTRPV subtypes.

Indexed as

Ion Channel GatingCytoplasmHEK293 CellsHumansModels, MolecularMutant ProteinsProtein DomainsProtein SubunitsTemperatureTRPV Cation ChannelsMutant ProteinsProtein SubunitsTRPV3 protein, humanTRPV Cation Channelscryo-electronmicroscopyelectrophysiologyhumanion channelligand dependent gatingmolecular biophysicssensitizationstructural biologyTRP channel

Identifiers

PMID31070581
PMCPMC6538378
OpenAlexW2943925785

What OpenQuestion holds

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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.