ArticleScientific reports2017
TRPV1 temperature activation is specifically sensitive to strong decreases in amino acid hydrophobicity.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- Review
- Relation between flexibility and intrinsically disorder regions in thermosensitive TRP channels reveal allosteric effects.European biophysics journal : EBJ · 2024Article
- Temperature-Dependent Activation of Thermosensitive Transient Receptor Potential Channels.Advances in experimental medicine and biology · 2024Review
- Transcending Markov: non-Markovian rate processes of thermosensitive TRP ion channels.Royal Society open science · 2023Article
- A molecular perspective on identifying TRPV1 thermosensitive regions and disentangling polymodal activation.Temperature (Austin, Tex.) · 2023Review
- Evolution of Transient Receptor Potential (TRP) Ion Channels in Antarctic Fishes (Cryonotothenioidea) and Identification of Putative Thermosensors.Genome biology and evolution · 2022Article
- A Systematical Survey on the TRP Channels Provides New Insight into Its Functional Diversity in Zhikong Scallop (International journal of molecular sciences · 2021Article
- Evidence that the TRPV1 S1-S4 membrane domain contributes to thermosensing.Nature communications · 2020Article
- A specialized pore turret in the mammalian cation channel TRPV1 is responsible for distinct and species-specific heat activation thresholds.The Journal of biological chemistry · 2020Article
- Comparative modelling studies of fruit bromelain using molecular dynamics simulation.Journal of molecular modeling · 2020Article
- A single TRPV1 amino acid controls species sensitivity to capsaicin.Scientific reports · 2020Article
- A paradigm of thermal adaptation in penguins and elephants by tuning cold activation in TRPM8.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Structural mechanisms of transient receptor potential ion channels.The Journal of general physiology · 2020Review
- Cytoplasmic Inter-Subunit Interface Controls Use-Dependence of Thermal Activation of TRPV3 Channel.International journal of molecular sciences · 2019Article
- Structural and Evolutionary Insights Point to Allosteric Regulation of TRP Ion Channels.Accounts of chemical research · 2019Article
- Heat activation mechanism of TRPV1: New insights from molecular dynamics simulation.Temperature (Austin, Tex.) · 2019Review
- Article
- Expression and Purification of the Pain Receptor TRPV1 for Spectroscopic Analysis.Scientific reports · 2017Article
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Authors and funding
3 authors.
Funding
Abstract
Several transient receptor potential (TRP) ion channels can be directly activated by hot or cold temperature with high sensitivity. However, the structures and molecular mechanism giving rise to their high temperature sensitivity are not fully understood. One hypothesized mechanism assumes that temperature activation is driven by the exposure of hydrophobic residues to solvent. This mechanism further predicts that residues are exposed to solvent in a coordinated fashion, but without necessarily being located in close proximity to each other. However, there is little experimental evidence supporting this mechanism in TRP channels. Here, we combined high-throughput mutagenesis, functional screening, and deep sequencing to identify mutations from a total of ~7,300 TRPV1 random mutant clones. We found that strong decreases in hydrophobicity of amino acids are better tolerated for activation by capsaicin than for activation by hot temperature, suggesting that strong hydrophobicity might be specifically required for temperature activation. Altogether, our work provides initial correlative support for a previously hypothesized temperature mechanism in TRP ion channels.
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