Evidence map›Paper›PMID 20351268›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2010

Thermosensitive TRP channel pore turret is part of the temperature activation pathway.

Fan Yang, Yuanyuan Cui, KeWei Wang, Jie Zheng

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 126 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
126citing papers in PubMed, 1 pooled it
–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

126 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Distinct functional open states of the polymodal nociceptor TRPV1.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. An Extracellular Pore‑Targeting Peptide Defines a Designable Allosteric Site in TRPV2.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  4. Article
  5. Journal of Zhejiang University. Science. B · 2026
    Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Protein dynamics underlies strong temperature dependence of heat receptors.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  12. Article
  13. Article
  14. Article
  15. 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
  16. Article
  17. Implications of a temperature-dependent heat capacity for temperature-gated ion channels.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  18. Article
  19. Article
  20. Review

66 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors.

Fan YangDepartment of Physiology and Membrane Biology, University of California Davis, Davis, CA 95616, USA.
Yuanyuan Cui
KeWei Wang
Jie Zheng

Funding

THE ACTIVATION GATE OF CYCLIC NUCLEOTIDE-GATED CHANNELSR21EY016754 · NEI · UNIVERSITY OF CALIFORNIA AT DAVIS · PI ZHENG, JIE · 2007 to 2008
$403k
NEI NIH HHS R21 EY016754PHS HHS REY016754A
6 · The paper itself

Abstract

Temperature sensing is crucial for homeotherms, including human beings, to maintain a stable body core temperature and respond to the ambient environment. A group of exquisitely temperature-sensitive transient receptor potential channels, termed thermoTRPs, serve as cellular temperature sensors. How thermoTRPs convert thermal energy (heat) into protein conformational changes leading to channel opening remains unknown. Here we demonstrate that the pathway for temperature-dependent activation is distinct from those for ligand- and voltage-dependent activation and involves the pore turret. We found that mutant channels with an artificial pore turret sequence lose temperature sensitivity but maintain normal ligand responses. Using site-directed fluorescence recordings we observed that temperature change induces a significant rearrangement of TRPV1 pore turret that is coupled to channel opening. This movement is specifically associated to temperature-dependent activation and is not observed during ligand- and voltage-dependent channel activation. These observations suggest that the turret is part of the temperature-sensing apparatus in thermoTRP channels, and its conformational change may give rise to the large entropy that defines high temperature sensitivity.

Indexed as

AnimalsBacterial ProteinsCell LineHot TemperatureHumansLigandsLuminescent ProteinsMiceModels, BiologicalProtein ConformationProtein Structure, TertiaryTemperatureThermodynamicsTRPC Cation ChannelsBacterial ProteinsLigandsLuminescent ProteinsTRPC Cation Channelsyellow fluorescent protein, Bacteria

Identifiers

PMID20351268
PMCPMC2872446

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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.