The ATP,Mg-dependent protein phosphatase: Regulation by casein kinase-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 PCS H1 phosphatase, but 10-fold less when purified in the presence of NaF, suggesting an in vivo phosphorylation of the casei...

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Bibliographic Details
Published in:FEBS letters 1987-11, Vol.224 (2), p.385-390
Main Authors: Agostinis, Patrizia, Vandenheede, Jackie R., Goris, Jozef, Meggio, Flavio, Pinna, Lorenzo A., Merlevede, Wilfried
Format: Article
Language:English
Subjects:
Analytical, structural and metabolic biochemistry
ATP,Mg-dependent phosphatase
ATP,Mg-dependent protein phosphatase
Biological and medical sciences
Casein kinase-1
Casein kinase-2
Casein Kinases
Enzyme Activation
Enzymes and enzyme inhibitors
Fundamental and applied biological sciences. Psychology
Hydrolases
Modulator subunit
Phosphoprotein Phosphatases - metabolism
Phosphoproteins - metabolism
Phosphorylation
Protein Kinases - physiology
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Summary: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 PCS H1 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 F A-mediated activation, while it does not impair the activated phosphatase.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(87)80489-1