Evidence map›Paper›PMID 25030910›Full record

ArticleeLife2014

High temperature sensitivity is intrinsic to voltage-gated potassium channels.

Fan Yang, Jie Zheng

Abstract read
In one paragraph

Article in eLife, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing 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

47 citing papers in PubMed.

  1. Article
  2. Article
  3. Mild Focal Cooling Decouples Dendrites to Reconfigure Cortical Output.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  4. Article
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  8. Mild focal cooling selectively impacts computations in dendritic trees.bioRxiv : the preprint server for biology · 2024
    Article
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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

2 authors.

Fan YangDepartment of Physiology and Membrane Biology, University of California, Davis School of Medicine, Davis, United States.
Jie ZhengDepartment of Physiology and Membrane Biology, University of California, Davis School of Medicine, Davis, United States jzheng@ucdavis.edu.

Funding

Molecular Mechanism of pH Regulation of TRPV1 ActivationR01NS072377 · NINDS · UNIVERSITY OF CALIFORNIA AT DAVIS · PI ZHENG, JIE · 2011 to 2015
$1.7M
NINDS NIH HHS R01 NS072377NINDS NIH HHS R01NS072377
6 · The paper itself

Abstract

Temperature-sensitive transient receptor potential (TRP) ion channels are members of the large tetrameric cation channels superfamily but are considered to be uniquely sensitive to heat, which has been presumed to be due to the existence of an unidentified temperature-sensing domain. Here we report that the homologous voltage-gated potassium (Kv) channels also exhibit high temperature sensitivity comparable to that of TRPV1, which is detectable under specific conditions when the voltage sensor is functionally decoupled from the activation gate through either intrinsic mechanisms or mutations. Interestingly, mutations could tune Shaker channel to be either heat-activated or heat-deactivated. Therefore, high temperature sensitivity is intrinsic to both TRP and Kv channels. Our findings suggest important physiological roles of heat-induced variation in Kv channel activities. Mechanistically our findings indicate that temperature-sensing TRP channels may not contain a specialized heat-sensor domain; instead, non-obligatory allosteric gating permits the intrinsic heat sensitivity to drive channel activation, allowing temperature-sensitive TRP channels to function as polymodal nociceptors.

Indexed as

Allosteric RegulationAnimalsGene ExpressionHEK293 CellsHot TemperatureHumansIon Channel GatingIon TransportLarge-Conductance Calcium-Activated Potassium ChannelsMembrane PotentialsMicePatch-Clamp TechniquesPotassiumProtein Structure, TertiaryShab Potassium ChannelsShaker Superfamily of Potassium ChannelsKcnb1 protein, mouseLarge-Conductance Calcium-Activated Potassium ChannelsPotassiumShab Potassium ChannelsShaker Superfamily of Potassium ChannelsShal Potassium ChannelsTRPV1 protein, mouseTRPV Cation Channelsallosteric couplingconformational changesgatingpotassium channeltemperature sensingTRP channel

Identifiers

PMID25030910
PMCPMC4123715

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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.