ArticleProceedings of the National Academy of Sciences of the United States of America2023
A suicidal mechanism for the exquisite temperature sensitivity of TRPV1.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 27 citations in OpenAlex.
- Thermodynamic coupling between cold and heat activations of TRPV2.Scientific reports · 2026Article
- CaCommunications biology · 2026Article
- Structural energetics of cold sensitivity.Nature · 2026Article
- Review
- Biological fundamental functional units of meridians: mechanosensitive ion channels.Frontiers in medicine · 2026Review
- TRPV2 and TRPC5 are potential targets for astringent phytochemicals.Current research in food science · 2026Article
- Mechanically induced dysregulation of calcium homeostasis: a molecular linchpin in asthmatic pathogenesis.European journal of medical research · 2025Review
- Thermoring basis for the proton-driven heat activation of a cation-selective channel in myriapods.Scientific reports · 2025Article
- Pathway-dependent cold activation of heat-responsive TRPV channels.Scientific reports · 2025Article
- Chikungunya Particle and RNA Induce Mechanical and Heat Hypersensitivities in a TRPV1-Dependent Manner.Biomolecules · 2025Article
- Protein dynamics underlies strong temperature dependence of heat receptors.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- ATP-dependent thermoring basis for the heat unfolding of the first nucleotide-binding domain isolated from human CFTR.Research square · 2024Article
- Oleic acid released by sensory neurons inhibits TRPV1-mediated thermal hypersensitivity via GPR40.iScience · 2024Article
- The Variety of Mechanosensitive Ion Channels in Retinal Neurons.International journal of molecular sciences · 2024Review
- Temperature gating in thermoTRPs may depend on temperature-dependent heat capacity differences.Temperature (Austin, Tex.) · 2024Article
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 2 countries.
Funding
Abstract
The vanilloid receptor TRPV1 is an exquisite nociceptive sensor of noxious heat, but its temperature-sensing mechanism is yet to define. Thermodynamics dictate that this channel must undergo an unusually energetic allosteric transition. Thus, it is of fundamental importance to measure directly the energetics of this transition in order to properly decipher its temperature-sensing mechanism. Previously, using submillisecond temperature jumps and patch-clamp recording, we estimated that the heat activation for TRPV1 opening incurs an enthalpy change on the order of 100 kcal/mol. Although this energy is on a scale unparalleled by other known biological receptors, the generally imperfect allosteric coupling in proteins implies that the actual amount of heat uptake driving the TRPV1 transition could be much larger. In this paper, we apply differential scanning calorimetry to directly monitor the heat flow in TRPV1 that accompanies its temperature-induced conformational transition. Our measurements show that heat invokes robust, complex thermal transitions in TRPV1 that include both channel opening and a partial protein unfolding transition and that these two processes are inherently coupled. Our findings support that irreversible protein unfolding, which is generally thought to be destructive to physiological function, is essential to TRPV1 thermal transduction and, possibly, to other strongly temperature-dependent processes in biology.
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Registered trials
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.