Transduction in taste receptor cells requires cAMP-dependent protein kinase

Nature. 1988 Jan 28;331(6154):351-4. doi: 10.1038/331351a0.


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 cAMP 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 cells. 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 olfactory and photoreceptor cells, where cyclic nucleotides control unspecific channels by binding to them rather than by inducing their phosphorylation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Action Potentials / drug effects
  • Adenosine Triphosphate / pharmacology
  • Animals
  • Calcium / pharmacology
  • Cyclic AMP / physiology*
  • Cyclic GMP / physiology
  • Ion Channels / drug effects
  • Ion Channels / metabolism
  • Protein Kinases / physiology*
  • Rana esculenta
  • Sucrose / pharmacology
  • Taste Buds / enzymology
  • Taste Buds / physiology*


  • Ion Channels
  • Sucrose
  • Adenosine Triphosphate
  • Cyclic AMP
  • Protein Kinases
  • Cyclic GMP
  • Calcium