ATP-sensitive K+ channels in a plasma membrane H+-ATPase mutant of the yeast Saccharomyces cerevisiae.
A mutant in the plasma membrane H+-ATPase gene of the yeast Saccharomyces cerevisiae with a reduced H+-ATPase activity, when examined at the single-channel level with the patch-clamp technique, was found to exhibit K+ channels activated by intracellular application of ATP. In the parent strain, the same channel, identified by its conductance and selectivity, is not activated by ATP. This activity in the mutant is blocked by the ATPase inhibitor N,N'-dicyclohexylcarbodiimide. ADP and the ATP analog adenosine 5'-[gamma-[35S]thio]triphosphate do not activate the channel. These findings suggest a tight physical coupling between the plasma membrane ATPase and the K+ channel.
Ramirez
J A
JA
Department of Biophysics, University of California, Berkeley 94720.
Vacata
V
V
McCusker
J H
JH
Haber
J E
JE
Mortimer
R K
RK
Owen
W G
WG
Lecar
H
H
D000255:Adenosine Triphosphate / Q000494:pharmacology*; D004024:Dicyclohexylcarbodiimide / Q000494:pharmacology; D004553:Electric Conductivity; D007700:Kinetics; D008433:Mathematics; D008962:Models, Theoretical; D009154:Mutation; D015221:Potassium Channels / Q000187:drug effects / Q000502:physiology*; D006180:Proton-Translocating ATPases / Q000235:genetics*; D012441:Saccharomyces cerevisiae / Q000201:enzymology / Q000235:genetics / Q000502:physiology*
D015221:Potassium Channels; D004024:Dicyclohexylcarbodiimide; D000255:Adenosine Triphosphate; D006180:Proton-Translocating ATPases