Covalent phosphorylation of the Mg2+-dependent ATPase of yeast plasma membranes.
Phosphorylation by [gamma-32P]ATP of proteins associated with the plasma membrane of Saccharomyces cerevisiae has been studied both in vivo and in vitro. Although at least nine proteins are labeled in vivo, there is only one major protein labeled in vitro. This species with an apparent molecular weight of 114,000 has been identified as the plasma membrane Mg2+-ATPase. Phosphorylation of this enzyme occurs exclusively on serine residues. This is the first report that the proton-translocating ATPase of fungal plasma membranes is subject to phosphorylation by a protein kinase.
D000251:Adenosine Triphosphatases / Q000378:metabolism*; D017301:Ca(2+) Mg(2+)-ATPase; D002462:Cell Membrane / Q000201:enzymology; D007700:Kinetics; D008565:Membrane Proteins / Q000378:metabolism*; D008970:Molecular Weight; D010761:Phosphorus Radioisotopes; D010766:Phosphorylation; D012441:Saccharomyces cerevisiae / Q000201:enzymology*
D008565:Membrane Proteins; D010761:Phosphorus Radioisotopes; D000251:Adenosine Triphosphatases; D017301:Ca(2+) Mg(2+)-ATPase