ArticleThe Journal of biological chemistry2013
Gating transitions in the palm domain of ASIC1a.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 32 citations in OpenAlex.
- Identification, characterization, and structure-activity relationship of the ASIC3-selective peptide WRPRFa.Communications chemistry · 2025Article
- Review
- Function and phylogeny support the independent evolution of an ASIC-like Deg/ENaC channel in the Placozoa.Communications biology · 2023Article
- Review
- Accessibility of ENaC extracellular domain central core residues.The Journal of biological chemistry · 2022Article
- Acid-sensing ion channel 3: An analgesic target.Channels (Austin, Tex.) · 2021Review
- Mutation of a conserved glutamine residue does not abolish desensitization of acid-sensing ion channel 1.The Journal of general physiology · 2021Article
- Evolution of acid nociception: ion channels and receptors for detecting acid.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2019Review
- Mutations in the palm domain disrupt modulation of acid-sensing ion channel 1a currents by neuropeptides.Scientific reports · 2019Article
- ASIC3 fine-tunes bladder sensory signaling.American journal of physiology. Renal physiology · 2018Article
- Mapping allosteric linkage to channel gating by extracellular domains in the human epithelial sodium channel.The Journal of biological chemistry · 2018Article
- Naked mole-rat acid-sensing ion channel 3 forms nonfunctional homomers, but functional heteromers.The Journal of biological chemistry · 2018Article
- Article
- The nonproton ligand of acid-sensing ion channel 3 activates mollusk-specific FaNaC channels via a mechanism independent of the native FMRFamide peptide.The Journal of biological chemistry · 2017Article
- Novel Insights into Acid-Sensing Ion Channels: Implications for Degenerative Diseases.Aging and disease · 2016Review
- The Thumb Domain Mediates Acid-sensing Ion Channel Desensitization.The Journal of biological chemistry · 2016Article
- Structural domains underlying the activation of acid-sensing ion channel 2a.Molecular pharmacology · 2015Article
- Proton-sensitive cation channels and ion exchangers in ischemic brain injury: new therapeutic targets for stroke?Progress in neurobiology · 2014Review
- Independent contribution of extracellular proton binding sites to ASIC1a activation.The Journal of biological chemistry · 2013Article
- Conformational changes in the lower palm domain of ASIC1a contribute to desensitization and RFamide modulation.PloS one · 2013Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
Acid-sensing ion channels (ASICs) are trimeric cation-selective proton-gated ion channels expressed in the central and peripheral nervous systems. The pore-forming transmembrane helices in these channels are linked by short loops to the palm domain in the extracellular region. Here, we explore the contribution to proton gating and desensitization of Glu-79 and Glu-416 in the palm domain of ASIC1a. Engineered Cys, Lys, and Gln substitutions at these positions shifted apparent proton affinity toward more acidic values. Double mutant cycle analysis indicated that Glu-79 and Glu-416 cooperatively facilitated pore opening in response to extracellular acidification. Channels bearing Cys at position 79 or 416 were irreversibly modified by thiol-reactive reagents in a state-dependent manner. Glu-79 and Glu-416 are located in β-strands 1 and 12, respectively. The covalent modification by (2-(trimethylammonium)ethyl) methanethiosulfonate bromide of Cys at position 79 impacted conformational changes associated with pore closing during desensitization, whereas the modification of Cys at position 416 affected conformational changes associated with proton gating. These results suggest that β-strands 1 and 12 contribute antagonistically to activation and desensitization of ASIC1a. Site-directed mutagenesis experiments indicated that the lower palm domain contracts in response to extracellular acidification. Taken together, our studies suggest that the lower palm domain mediates conformational movements that drive pore opening and closing events.
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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.