Signalling in taste receptor cells: cAMP-dependent protein kinase causes depolarization by closure of 44 pS K-channels.
1. In whole-cell patch-clamp recordings cytosolic cAMP causes a substantial depolarization of taste receptor cells isolated from the frog tongue. The depolarization requires the presence of ATP in the cell and is suppressed by protein kinase inhibitor. 2. The depolarization also develops in the absence of cAMP while the catalytic subunit of the kinase is allowed to diffuse into the cell in the presence of ATP. 3. In membrane patches excised from these cells the catalytic subunit is found to inactivate K-channels of 44 pS conductance, presumably by phosphorylation. 4. It appears that cAMP is one of the intracellular messengers in gustatory chemoreception, and that it causes membrane depolarization through activation of a protein kinase which controls the activity of one set of K-channels.
D000818:Animals; D008564:Membrane Potentials; D015221:Potassium Channels / Q000502:physiology*; D011494:Protein Kinases / Q000502:physiology*; D011893:Rana esculenta; D013650:Taste Buds / Q000166:cytology / Q000502:physiology*
D015221:Potassium Channels; D011494:Protein Kinases