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Aromatic amino acids in the finger domain of the FMRFamide-gated Na$$^+$$ channel are involved in the FMRFamide recognition and the activation
Open accessPublished version of a preprint
Abstract
FMRFamide-gated Na+ channel (FaNaC) is a member of the DEG/ENaC family and activated by a neuropeptide, FMRFamide. Structural information about the FMRFamide-dependent gating is, however, still elusive. Because two phenylalanines of FMRFamide are essential for the activation of FaNaC, we hypothesized that aromatic-aromatic interaction between FaNaC and FMRFamide is critical for FMRFamide recognition and/or the activation gating. Here, we focused on eight conserved aromatic residues in the finger domain of FaNaCs and tested our hypothesis by mutagenic analysis and in silico docking simulations. The mutation of conserved aromatic residues in the finger domain reduced the FMRFamide potency, suggesting that the conserved aromatic residues are involved in the FMRFamide-dependent activation. The kinetics of the FMRFamide-gated currents were also modified substantially in some mutants. Some results of docking simulations were consistent with a hypothesis that the aromatic-aromatic interaction between the aromatic residues in FaNaC and FMRFamide is involved in the FMRFamide recognition. Collectively, our results suggest that the conserved aromatic residues in the finger domain of FaNaC are important determinants of the ligand recognition and/or the activation gating in FaNaC.
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Metadata
- Authors
- Furukawa, Y., & Tagashira, I.
- Affiliations
- Hiroshima University (JP)
- Corresponding author
- Furukawa, Yasuo
- ORCID
- Furukawa, Yasuo
- Venue
- Pflügers Archiv - European Journal of Physiology
- Published
- 2023-06-08
- Volume
- 475
- Issue
- 8
- Pages
- 975-993
- ISSN
- 0031-6768 (ISSN-L)
- 1432-2013
- OpenAlex
- W4379768709
- Cited by
- 4
- References
- 54
- Citations by year
- 2025: 2 · 2024: 2
- FWCI
- 0.36
- Type
- journal article
- Language
- en
- Open access
- green
- dx.doi.org
- Licence
- www.springernature.com/gp/researchers/text-and-data-mining (tdm)
- www.springernature.com/gp/researchers/text-and-data-mining (vor)
- Locations
- Pflügers Archiv - European Journal of Physiology (publishedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- PubMed (publishedVersion)
- Funders
- Japan Society for the Promotion of Science (15K07149)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion channel regulation and function
- Life Sciences › Neuroscience › Sensory Systems › Ion Channels and Receptors
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nicotinic Acetylcholine Receptors Study
- Keywords
- finger domain, aromatic amino acids, aromatic-aromatic interactions, conserved residues, site-directed mutagenesis, molecular docking
- MeSH terms
- Sodium Channels, FMRFamide, Amino Acids, Aromatic
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