ArticleScientific reports2019
Mutations in the palm domain disrupt modulation of acid-sensing ion channel 1a currents by neuropeptides.
Article in Scientific reports, 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, 23 citations in OpenAlex.
- Identification, characterization, and structure-activity relationship of the ASIC3-selective peptide WRPRFa.Communications chemistry · 2025Article
- Flipped binding modes for the same agonist in closely related neuropeptide-gated ion channels.Biophysical journal · 2025Article
- Structural basis for excitatory neuropeptide signaling.Nature structural & molecular biology · 2024Article
- Structure and mechanism of a neuropeptide-activated channel in the ENaC/DEG superfamily.Nature chemical biology · 2023Article
- Aromatic amino acids in the finger domain of the FMRFamide-gated NaPflugers Archiv : European journal of physiology · 2023Article
- Comparative analysis defines a broader FMRFamide-gated sodium channel family and determinants of neuropeptide sensitivity.The Journal of biological chemistry · 2022Article
- Changes in HFrontiers in cellular neuroscience · 2021Article
- Sevanol and Its Analogues: Chemical Synthesis, Biological Effects and Molecular Docking.Pharmaceuticals (Basel, Switzerland) · 2020Article
- Mechanism and site of action of big dynorphin on ASIC1a.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- A NaThe Journal of biological chemistry · 2019Article
- Sa12b Peptide from Solitary Wasp Inhibits ASIC Currents in Rat Dorsal Root Ganglion Neurons.Toxins · 2019Article
- Accelerated Current Decay Kinetics of a Rare Human Acid-Sensing ion Channel 1a Variant That Is Used in Many Studies as Wild Type.Frontiers in molecular neuroscience · 2019Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Modulation by neuropeptides enhances several functions of acid-sensing ion channels (ASICs), such as pain sensation and acid-induced neuronal injury. The acid-induced opening of ASICs is transient, because of a rapid desensitization. Neuropeptides containing an Arg-Phe-amide motif affect ASIC desensitization and allow continuous activity of ASICs. In spite of the importance of the sustained ASIC activity during prolonged acidification, the molecular mechanisms of ASIC modulation by neuropeptides is only poorly understood. To identify the FRRFa (Phe-Arg-Arg-Phe-amide) binding site on ASIC1a, we carried out an in silico docking analysis and verified functionally the docking predictions. The docking experiments indicated three possible binding pockets, located (1) in the acidic pocket between the thumb, finger, β-ball and palm domains, (2) in a pocket at the bottom of the thumb domain, and (3) in the central vestibule along with the connected side cavities. Functional measurements of mutant ASIC1a confirmed the importance of residues of the lower palm, which encloses the central vestibule and its side cavities, for the FRRFa effects. The combined docking and functional experiments strongly suggest that FRRFa binds to the central vestibule and its side cavities to change ASIC desensitization.
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