FMRFamide-gated Na+ channel (FaNaC) is the only known peptide-gated ion channel, which belongs to the epithelial Na+ channel/degenerin (ENaC/DEG) family. We have cloned a putative FaNaC from the Aplysia kurodai CNS library using PCR, and examined its characteristics in Xenopus oocytes. A. kurodai FaNaC (AkFaNaC) comprised with 653 amino acids, and the sequence predicts two putative membrane domains and a large extracellular domain as in other members of the ENaC/DEG family. In oocytes expressing AkFaNaC, FMRFamide evoked amiloride-sensitive Na+ current. Different from the known FaNaCs (Helix and Helisoma FaNaCs), AkFaNaC was blocked by external Ca2+ but not by Mg2+. Also, desensitization of the current was enhanced by Mg2+ but not by Ca2+. The FMRFamide-gated current was depressed in both low and high pH. These results indicate that AkFaNaC is an FaNaC of Aplysia, and that the channel has Aplysia specific functional domains.
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Aromatic amino acids in the finger domain of the FMRFamide-gated Na[Formula: see text] channel are involved in the FMRFamide recognition and the activation.
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Laboratory of Neurobiology, Graduate School of Integrated Arts and Sciences, Hiroshima University, Kagamiyama 1-7-1, Higashi-Hiroshima 739-8521, Japan.
FMRFamide-gated Na(+) channel (FaNaC) is a peptide-gated sodium channel in the epithelial Na(+) channel/degenerin family. Although there are some data on the location of the putative peptide binding site, there is no structural information on the activation gating of FaNaC. Here, we addressed the function of a conserved aspartate residue in the second transmembrane domain of FaNaC.
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