Agostinis P, Vandenheede J R, Goris J, Meggio F, Pinna L A, Merlevede W
Afdeling Biochemie, Faculteit Geneeskunde, Katholieke Universiteit te Leuven, Belgium.
FEBS Lett. 1987 Nov 30;224(2):385-90. doi: 10.1016/0014-5793(87)80489-1.
The free modulator subunit of the ATP,Mg-dependent phosphatase is phosphorylated up to 1 mol per mol by casein kinase-1, up to 1.85 mol per mol after dephosphorylation by the PCSH1 phosphatase, but 10-fold less when purified in the presence of NaF, suggesting an in vivo phosphorylation of the casein kinase-1 sites. Peptide mapping of 32P-modulator labeled by casein kinase-1 or -2 shows a different phosphorylation pattern. Phosphorylation of the inactive phosphatase by casein kinase-1 prevents the subsequent kinase FA-mediated activation, while it does not impair the activated phosphatase.
ATP、Mg依赖性磷酸酶的游离调节亚基被酪蛋白激酶-1磷酸化，每摩尔可达1摩尔，经PCSH1磷酸酶去磷酸化后，每摩尔可达1.85摩尔，但在氟化钠存在下纯化时，磷酸化程度降低10倍，这表明酪蛋白激酶-1位点存在体内磷酸化。用酪蛋白激酶-1或-2标记的32P调节亚基的肽图谱显示出不同的磷酸化模式。酪蛋白激酶-1对无活性磷酸酶的磷酸化可阻止随后激酶FA介导的激活，而对活化的磷酸酶则无损害。
