Abstract
Neurotransmitters modulate the activity of ion channels through a variety of second messengers, including cyclic AMP1–4, cyclic GMP5,6 and the products of phosphatidylinositol breakdown7–9. Little is known about how different transmitters acting through different second-messenger systems interact within a cell to regulate single ion channels. We here describe the reciprocal actions of serotonin and the molluscan neuropeptide, FMRFamide10, on individual K+ channels in Aplysia sensory neurons. In these cells, serotonin causes prolonged all-or-none closure of a class of background conductance K+ channels (the S channels)11 through cAMP-dependent protein phosphorylation12–14. Using single-channel recording, we have found that FMRFamide produces two actions on the S channels; it increases the probablity of opening of the S channels via a cAMP-independent second-messenger system and it reverses the closures of S channels produced by serotonin or cAMP.
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Belardetti, F., Kandel, E. & Siegelbaum, S. Neuronal inhibition by the peptide FMRFamide involves opening of S K+ channels. Nature 325, 153–156 (1987). https://doi.org/10.1038/325153a0
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DOI: https://doi.org/10.1038/325153a0
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