Activation of yeast plasma membrane ATPase by phorbol ester.
Addition of 12-O-tetradecanoylphorbol-13-acetate (TPA) to yeast cells produces a 2-fold activation of the plasma membrane ATPase. The activation is reversible and time-and dose-dependent. The activated enzyme shows an increased affinity for its substrate, ATP, and its optimum pH is shifted to a more alkaline range. These changes are similar to those observed in the reported activation by glucose. Upon incubation of yeast cells with 32Pi incorporation of radioactivity in a membrane polypeptide of 105 kDa is observed after addition of either glucose or TPA.
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000378:metabolism; D002462:Cell Membrane / Q000201:enzymology; D000242:Cyclic AMP / Q000378:metabolism; D004789:Enzyme Activation / Q000187:drug effects; D005947:Glucose / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008565:Membrane Proteins / Q000378:metabolism; D010704:Phorbols / Q000494:pharmacology*; D010766:Phosphorylation; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D013755:Tetradecanoylphorbol Acetate / Q000494:pharmacology*
D008565:Membrane Proteins; D010704:Phorbols; D000255:Adenosine Triphosphate; D000242:Cyclic AMP; D000251:Adenosine Triphosphatases; D005947:Glucose; D013755:Tetradecanoylphorbol Acetate