ArticleBiophysical journal2020
The Contribution of the Ankyrin Repeat Domain of TRPV1 as a Thermal Module.
Article in Biophysical journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 40 citations in OpenAlex.
- TRPV1 and TRPA1 channels exhibit bifurcated sensing of singlet oxygen and hydrogen peroxide.Redox biology · 2026Article
- Review
- Perspectives on TRPV Channels in the Structural and Computational Revolution Era.Advances in experimental medicine and biology · 2026Review
- Temperature-induced structural changes in thermosensitive transient receptor potential channels (thermoTRPs).Frontiers in molecular neuroscience · 2026Review
- Comparing cryo-EM methods and molecular dynamics simulation to investigate heterogeneity in ligand-bound TRPV1.Nature communications · 2025Article
- 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
- Missense variant analysis in the TRPV1 ARD reveals the unexpected functional significance of a methionine.PloS one · 2025Article
- Article
- Article
- Temperature sensitive contact modes allosterically gate TRPV3.PLoS computational biology · 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
- Real-Time Observation of Capsaicin-Induced Intracellular Domain Dynamics of TRPV1 Using the Diffracted X-ray Tracking Method.Membranes · 2023Article
- Two single-point mutations in Ankyrin Repeat one drastically change the threshold temperature of TRPV1.Nature communications · 2023Article
- Targeting TRP channels: recent advances in structure, ligand binding, and molecular mechanisms.Frontiers in molecular neuroscience · 2023Review
- A molecular perspective on identifying TRPV1 thermosensitive regions and disentangling polymodal activation.Temperature (Austin, Tex.) · 2023Review
- Emerging role of transient receptor potential (TRP) ion channels in cardiac fibroblast pathophysiology.Frontiers in physiology · 2022Review
- Identification of a helix-turn-helix motif for high temperature dependence of vanilloid receptor TRPV2.The Journal of physiology · 2021Article
- Heat-dependent opening of TRPV1 in the presence of capsaicin.Nature structural & molecular biology · 2021Article
- 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
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The TRPV1 cation nonselective ion channel plays an essential role in thermosensation and perception of other noxious stimuli. TRPV1 can be activated by low extracellular pH, high temperature, or naturally occurring pungent molecules such as allicin, capsaicin, or resiniferatoxin. Its noxious thermal sensitivity makes it an important participant as a thermal sensor in mammals. However, details of the mechanism of channel activation by increases in temperature remain unclear. Here, we used a combination of approaches to try to understand the role of the ankyrin repeat domain (ARD) in channel behavior. First, a computational modeling approach by coarse-grained molecular dynamics simulation of the whole TRPV1 embedded in a phosphatidylcholine and phosphatidylethanolamine membrane provides insight into the dynamics of this channel domain. Global analysis of the structural ensemble shows that the ARD is a region that sustains high fluctuations during dynamics at different temperatures. We then performed biochemical and thermal stability studies of the purified ARD by the means of circular dichroism and tryptophan fluorescence and demonstrate that this region undergoes structural changes at similar temperatures that lead to TRPV1 activation. Our data suggest that the ARD is a dynamic module and that it may participate in controlling the temperature sensitivity of TRPV1.
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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.