Abstract
In taste chemoreception, cyclic adenosine monophosphate (cAMP) appears to be one of the intracellular messengers coupling reception of stimulus to the generation of the response. The recent finding that sweet agents cause a GTP-dependent generation of cAMP1 poses the question of how this cytosolic messenger acts at the membrane of taste receptor cells. We have shown that cAMP causes a substantial depolarization in these cells2. Here we show with whole-cell recordings and inside-out membrane patches that the depolarization caused by cAMP is accounted for by the action of cAMP-dependent protein kinase, which inactivates potassium channels predominantly of 44 pS conductance. Thus, intracellular signalling of the gustatory cells differs from that of olfactory3 and photoreceptor cells4,5, where cyclic nucleotides control unspecific channels by binding to them rather than by inducing their phosphorylation.
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Avenet, P., Hofmann, F. & Lindemann, B. Transduction in taste receptor cells requires cAMP-dependent protein kinase. Nature 331, 351–354 (1988). https://doi.org/10.1038/331351a0
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DOI: https://doi.org/10.1038/331351a0
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