ArticleNature structural & molecular biology2024
Structural basis of TRPV1 modulation by endogenous bioactive lipids.
Article in Nature structural & molecular biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed.
- A topical nociceutical formulation ameliorates chemotherapy-induced peripheral neuropathy: a pilot randomized clinical study.Clinical & translational oncology : official publication of the Federation of Spanish Oncology Societies and of the National Cancer Institute of Mexico · 2026Trial
- Orally available Colivin traps TRPV3 in an inactive state and suppresses intestinal inflammation.The EMBO journal · 2026Article
- LIPUS combined with mild hyperthermia promotes rotator cuff healing via TRPV1/CaJournal of orthopaedic translation · 2026Article
- Structural diversity of heat-sensing channel TRPV3 with Olmsted syndrome mutations.Nature communications · 2026Article
- Thermodynamic coupling between cold and heat activations of TRPV2.Scientific reports · 2026Article
- Structural energetics of cold sensitivity.Nature · 2026Article
- TRPV1 antagonism occurs through diverse structural mechanisms.bioRxiv : the preprint server for biology · 2026Article
- Stereoselectivity and functional plasticity of a common ligand-binding pocket in TRPM3.Nature communications · 2026Article
- Temperature-dependent gating pathways in TRPV3.Scientific reports · 2026Article
- Review
- Review
- The Nanodisc System for Investigating Protein-Lipid Interactions.Methods in molecular biology (Clifton, N.J.) · 2026Review
- Structural landscape of activation, desensitization and inhibition in the human TRPM4 channel.Nature structural & molecular biology · 2026Article
- Mechanism of capsaicin entry into buried vanilloid sites in TRPV1.Nature chemical biology · 2025Article
- Membrane-forming phospholipids allosterically modulate native-state prolyl isomerization in a CNG channel.Protein science : a publication of the Protein Society · 2025Article
- Pathway-dependent cold activation of heat-responsive TRPV channels.Scientific reports · 2025Article
- Cardiolipin dynamics promote membrane remodeling by mitochondrial OPA1.Nature communications · 2025Article
- Glucose-Facilitated Nanomicelles Cross Peripheral Nerve Barriers to Achieve Drug Delivery to Nerves.Advanced functional materials · 2025Article
- Structural basis of the inhibition of TRPV1 by analgesic sesquiterpenes.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Pharmacological evaluation of physcion as a TRPV1 inhibitor with multimodal analgesic efficacy in experimental pain models.Biological research · 2025Article
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Authors and funding
6 authors.
Funding
Abstract
TRP ion channels are modulated by phosphoinositide lipids, but the underlying structural mechanisms remain unclear. The capsaicin- and heat-activated receptor, TRPV1, has served as a model for deciphering lipid modulation, which is relevant to understanding how pro-algesic agents enhance channel activity in the setting of inflammatory pain. Identification of a pocket within the TRPV1 transmembrane core has provided initial clues as to how phosphoinositide lipids bind to and regulate the channel. Here we show that this regulatory pocket in rat TRPV1 can accommodate diverse lipid species, including the inflammatory lipid lysophosphatidic acid, whose actions are determined by their specific modes of binding. Furthermore, we show that an empty-pocket channel lacking an endogenous phosphoinositide lipid assumes an agonist-like state, even at low temperature, substantiating the concept that phosphoinositide lipids serve as negative TRPV1 modulators whose ejection from the binding pocket is a critical step toward activation by thermal or chemical stimuli.
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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.