ArticleThe journal of physiological sciences : JPS2014
Electrostatic charge at position 552 affects the activation and permeation of FMRFamide-gated Na+ channels.
Article in The journal of physiological sciences : JPS, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- 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
- Modulation of the FMRFamide-gated NaPflugers Archiv : European journal of physiology · 2017Article
- Exploration of the Peptide Recognition of an Amiloride-sensitive FMRFamide Peptide-gated Sodium Channel.The Journal of biological chemistry · 2016Article
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2 authors.
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Abstract
The FMRFamide-gated Na(+) channel (FaNaC) is a unique peptide-gated sodium channel and a member of the epithelial sodium channel/degenerin family. Previous studies have shown that an aspartate residue (Asp(552)) in the second transmembrane domain is involved in activation of the FaNaC. To examine the significance of a negative charge at position 552, we used a cysteine-modification method. Macroscopic currents of a cysteine mutant (D552C) were potentiated or inhibited by use of positively or negatively charged sulfhydryl reagents ([2-(trimethylammonium)ethyl]methanethiosulfonate bromide, MTSET, and sodium (2-sulfonatoethyl)methanethiosulfonate, MTSES, respectively). Dose-response analysis showed that treatment with MTSET increased the potency of the FMRFamide in the FaNaC whereas treatment with MTSES reduced the maximum response. Negative charge at position 552 was necessary for the characteristic inward rectification of the FaNaC. These results suggest that negative electric charge at position 552 is important to the activation and permeation properties of the FaNaC.
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