ArticleThe Journal of general physiology2022
Structural determinants of acid-sensing ion channel potentiation by single chain lipids.
Article in The Journal of general physiology, 2022. 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, 18 citations in OpenAlex.
- Lipid Regulation of Mechanosensitive Ion Channels.International journal of molecular sciences · 2026Review
- PUFA modulation of ASIC3 involves both specific and lipid solvent-like interactions.bioRxiv : the preprint server for biology · 2026Article
- Simulated Microgravity Causes Delayed Platelet Activation and Downregulates Acid-Sensing Ion Channel 1/2 Protein Expression.Biomedicines · 2025Article
- The bile acid-sensitive ion channel is gated by CaNature communications · 2025Article
- Molecular Insights into Single-Chain Lipid Modulation of Acid-Sensing Ion Channel 3.The journal of physical chemistry. B · 2024Article
- Molecular Insights into Single Chain Lipid Modulation of Acid-Sensing Ion Channel 3.bioRxiv : the preprint server for biology · 2024Article
- Editorial: ASICs: structure, function, and pharmacology, part II.Frontiers in physiology · 2024Article
- Article
- A loosely coordinated interaction site for arachidonic acid on ASICs.The Journal of general physiology · 2023Article
- Multiscale molecular dynamics simulations predict arachidonic acid binding sites in human ASIC1a and ASIC3 transmembrane domains.The Journal of general physiology · 2023Article
- Review
- ASIC3, a proton-gated ion channel with preference for polyunsaturated lipids with specific headgroup and tail properties.The Journal of general physiology · 2022Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Acid-sensing ion channels (ASICs) are sensitized to activation by inflammatory mediators such as the polyunsaturated fatty acid (PUFA) arachidonic acid (AA). Previous work has shown that AA can potentiate ASIC currents at subsaturating proton concentrations, but the structural mechanisms of this change in gating are not understood. Here we show that PUFAs cause multiple gating changes in ASIC3, including shifting the pH dependence of activation, slowing the rate of desensitization, and increasing the current even at a saturating pH. The impact on gating depends on the nature of both the head and tail of the lipid, with the head group structure primarily determining the magnitude of the effect on the channel. An N-acyl amino acid (NAAA), arachidonyl glycine (AG), is such a strong regulator that it can act as a ligand at neutral pH. Mutation of an arginine in the outer segment of TM1 (R64) eliminated the effect of docosahexaenoic acid (DHA) even at high concentrations, suggesting a potential interaction site for the lipid on the channel. Our results suggest a model in which PUFAs bind to ASICs via both their tail group and an electrostatic interaction between the negatively charged PUFA head group and the positively charged arginine side chain. These data provide the first look at the structural features of lipids that are important for modulating ASICs and suggest a potential binding site for PUFAs on the channel.
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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.