ArticleInternational journal of molecular sciences2019
Cytoplasmic Inter-Subunit Interface Controls Use-Dependence of Thermal Activation of TRPV3 Channel.
Article in International journal of molecular sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 21 citations in OpenAlex.
- Thermodynamic coupling between cold and heat activations of TRPV2.Scientific reports · 2026Article
- Temperature-induced structural changes in thermosensitive transient receptor potential channels (thermoTRPs).Frontiers in molecular neuroscience · 2026Review
- TRPV2 and TRPC5 are potential targets for astringent phytochemicals.Current research in food science · 2026Article
- Pathway-dependent cold activation of heat-responsive TRPV channels.Scientific reports · 2025Article
- TRPV3 in skin thermosensation and temperature responses.The journal of physiological sciences : JPS · 2025Review
- Thermoring basis for the TRPV3 bio-thermometer.Scientific reports · 2023Article
- Mutagenesis studies of TRPV1 subunit interfaces informed by genomic variant analysis.Biophysical journal · 2023Article
- Mechanisms of proton inhibition and sensitization of the cation channel TRPV3.The Journal of general physiology · 2021Article
- Current View of Ligand and Lipid Recognition by the Menthol Receptor TRPM8.Trends in biochemical sciences · 2020Review
- TRP Channels, Conformational Flexibility, and the Lipid Membrane.The Journal of membrane biology · 2020Review
- Article
- Structural biology of thermoTRPV channels.Cell calcium · 2019Review
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
The vanilloid transient receptor potential channel TRPV3 is a putative molecular thermosensor widely considered to be involved in cutaneous sensation, skin homeostasis, nociception, and pruritus. Repeated stimulation of TRPV3 by high temperatures above 50 °C progressively increases its responses and shifts the activation threshold to physiological temperatures. This use-dependence does not occur in the related heat-sensitive TRPV1 channel in which responses decrease, and the activation threshold is retained above 40 °C during activations. By combining structure-based mutagenesis, electrophysiology, and molecular modeling, we showed that chimeric replacement of the residues from the TRPV3 cytoplasmic inter-subunit interface (N251-E257) with the homologous residues of TRPV1 resulted in channels that, similarly to TRPV1, exhibited a lowered thermal threshold, were sensitized, and failed to close completely after intense stimulation. Crosslinking of this interface by the engineered disulfide bridge between substituted cysteines F259C and V385C (or, to a lesser extent, Y382C) locked the channel in an open state. On the other hand, mutation of a single residue within this region (E736) resulted in heat resistant channels. We propose that alterations in the cytoplasmic inter-subunit interface produce shifts in the channel gating equilibrium and that this domain is critical for the use-dependence of the heat sensitivity of TRPV3.
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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.