ArticlePloS one2013
Single residues in the outer pore of TRPV1 and TRPV3 have temperature-dependent conformations.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed.
- Expression and functional characterization of the TRPV3 channel in domestic cat (Felis catus) mature oocytes.Biological research · 2026Article
- Temperature-induced structural changes in thermosensitive transient receptor potential channels (thermoTRPs).Frontiers in molecular neuroscience · 2026Review
- Pathway-dependent cold activation of heat-responsive TRPV channels.Scientific reports · 2025Article
- Protein dynamics underlies strong temperature dependence of heat receptors.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Vertebrate behavioral thermoregulation: knowledge and future directions.Neurophotonics · 2024Review
- Relation between flexibility and intrinsically disorder regions in thermosensitive TRP channels reveal allosteric effects.European biophysics journal : EBJ · 2024Article
- Pathogenesis and management ofFrontiers in genetics · 2024Review
- Thermoring basis for the TRPV3 bio-thermometer.Scientific reports · 2023Article
- A suicidal mechanism for the exquisite temperature sensitivity of TRPV1.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- FRET analysis of the temperature-induced structural changes in human TRPV3.Scientific reports · 2023Article
- Thermoring basis for the TRPV3 bio-thermometer.Research square · 2023Article
- Two single-point mutations in Ankyrin Repeat one drastically change the threshold temperature of TRPV1.Nature communications · 2023Article
- TRPV3: Structure, Diseases and Modulators.Molecules (Basel, Switzerland) · 2023Review
- Identification of a helix-turn-helix motif for high temperature dependence of vanilloid receptor TRPV2.The Journal of physiology · 2021Article
- A Systematical Survey on the TRP Channels Provides New Insight into Its Functional Diversity in Zhikong Scallop (International journal of molecular sciences · 2021Article
- Structural mechanism of heat-induced opening of a temperature-sensitive TRP channel.Nature structural & molecular biology · 2021Article
- Heat-dependent opening of TRPV1 in the presence of capsaicin.Nature structural & molecular biology · 2021Article
- Article
- Gating of human TRPV3 in a lipid bilayer.Nature structural & molecular biology · 2020Article
- Structural mechanisms of transient receptor potential ion channels.The Journal of general physiology · 2020Review
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3 authors.
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Abstract
Thermosensation is mediated by ion channels that are highly temperature-sensitive. Several members of the family of transient receptor potential (TRP) ion channels are activated by cold or hot temperatures and have been shown to function as temperature sensors in vivo. The molecular mechanism of temperature-sensitivity of these ion channels is not understood. A number of domains or even single amino acids that regulate temperature-sensitivity have been identified in several TRP channels. However, it is unclear what precise conformational changes occur upon temperature activation. Here, we used the cysteine accessibility method to probe temperature-dependent conformations of single amino acids in TRP channels. We screened over 50 amino acids in the predicted outer pore domains of the heat-activated ion channels TRPV1 and TRPV3. In both ion channels we found residues that have temperature-dependent accessibilities to the extracellular solvent. The identified residues are located within the second predicted extracellular pore loop. These residues are identical or proximal to residues that were shown to be specifically required for temperature-activation, but not chemical activation. Our data precisely locate conformational changes upon temperature-activation within the outer pore domain. Collectively, this suggests that these specific residues and the second predicted pore loop in general are crucial for the temperature-activation mechanism of these heat-activated thermoTRPs.
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