Evidence map›Paper›PMID 32820172›Full record

ArticleNature communications2020

Evidence that the TRPV1 S1-S4 membrane domain contributes to thermosensing.

Minjoo Kim, Nicholas J Sisco, Jacob K Hilton, Camila M Montano, Manuel A Castro, Brian R Cherry, Marcia Levitus, Wade D Van Horn

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.0field-weighted citation impact, top 11% 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

28 citing papers in PubMed, 60 citations in OpenAlex.

  1. Article
  2. Article
  3. TRPV1 antagonism occurs through diverse structural mechanisms.bioRxiv : the preprint server for biology · 2026
    Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Protein dynamics underlies strong temperature dependence of heat receptors.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  11. Update on the Role of β2AR and TRPV1 in Respiratory Diseases.International journal of molecular sciences · 2024
    Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. A suicidal mechanism for the exquisite temperature sensitivity of TRPV1.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  19. Review
  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 2 institutions in 1 country.

Minjoo Kim *School of Molecular Sciences, Arizona State University, 551 E. University Drive, Tempe, AZ, 85287, USA.ORCID http://orcid.org/0000-0001-8032-2445
Nicholas J Sisco *School of Molecular Sciences, Arizona State University, 551 E. University Drive, Tempe, AZ, 85287, USA.
Jacob K HiltonSchool of Molecular Sciences, Arizona State University, 551 E. University Drive, Tempe, AZ, 85287, USA.
Camila M MontanoThe Biodesign Institute Virginia G. Piper Center for Personalized Diagnostics, Arizona State University, Tempe, AZ, 85287, USA.
Manuel A CastroSchool of Molecular Sciences, Arizona State University, 551 E. University Drive, Tempe, AZ, 85287, USA.ORCID http://orcid.org/0000-0001-9569-6116
Brian R CherryThe Magnetic Resonance Research Center, Arizona State University, Tempe, AZ, 85287, USA.
Marcia LevitusSchool of Molecular Sciences, Arizona State University, 551 E. University Drive, Tempe, AZ, 85287, USA.
Wade D Van HornSchool of Molecular Sciences, Arizona State University, 551 E. University Drive, Tempe, AZ, 85287, USA. wade.van.horn@asu.edu.ORCID http://orcid.org/0000-0002-2493-5578
Arizona State University · USResonance Research (United States) · US

Funding

PIRT Family Modulation of TRPM8R01GM112077 · NIGMS · ARIZONA STATE UNIVERSITY-TEMPE CAMPUS · PI VAN HORN, WADE D. · 2015 to 2019
$1.5M
NIGMS NIH HHS R01 GM112077
6 · The paper itself

Abstract

Sensing and responding to temperature is crucial in biology. The TRPV1 ion channel is a well-studied heat-sensing receptor that is also activated by vanilloid compounds, including capsaicin. Despite significant interest, the molecular underpinnings of thermosensing have remained elusive. The TRPV1 S1-S4 membrane domain couples chemical ligand binding to the pore domain during channel gating. Here we show that the S1-S4 domain also significantly contributes to thermosensing and couples to heat-activated gating. Evaluation of the isolated human TRPV1 S1-S4 domain by solution NMR, far-UV CD, and intrinsic fluorescence shows that this domain undergoes a non-denaturing temperature-dependent transition with a high thermosensitivity. Further NMR characterization of the temperature-dependent conformational changes suggests the contribution of the S1-S4 domain to thermosensing shares features with known coupling mechanisms between this domain with ligand and pH activation. Taken together, this study shows that the TRPV1 S1-S4 domain contributes to TRPV1 temperature-dependent activation.

Indexed as

Hot TemperatureBinding SitesCapsaicinCircular DichroismHumansIon Channel GatingMagnetic Resonance SpectroscopyModels, MolecularProtein BindingProtein DomainsThermosensingTRPV Cation ChannelsCapsaicinTRPV1 protein, humanTRPV Cation Channels

Identifiers

PMID32820172
PMCPMC7441067
OpenAlexW3055009501

What OpenQuestion holds

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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.