Phosphorylation of the phosphatase modulator subunit (inhibitor-2) by casein kinase-1. Identification of the phosphorylation sites.
The isolated modulator subunit of the inactive protein phosphatase-1 is phosphorylated in vitro by casein kinase-1 at two different sites: Ser-86 and Ser-174. The Ser-86 site is a common target for casein kinase-1 and casein kinase-2, but is preferentially phosphorylated by the former enzyme. The Ser-174 site seems to be specific for casein kinase-1, and is phosphorylated at a slower rate. These results give a new insight into the in vitro phosphorylation pattern of the modulator subunit of the phosphatase and provides additional data on the specificity of casein kinase-1.
Agostinis
P
P
Afdeling Biochemie, Faculteit Geneeskunde, Katholieke Universiteit te Leuven, Belgium.
Marin
O
O
James
P
P
Hendrix
P
P
Merlevede
W
W
Vandenheede
J R
JR
Pinna
L A
LA
D000595:Amino Acid Sequence; D000818:Animals; D047388:Casein Kinases; D002851:Chromatography, High Pressure Liquid; D008969:Molecular Sequence Data; D009132:Muscles / Q000201:enzymology; D010449:Peptide Mapping; D010749:Phosphoprotein Phosphatases / Q000737:chemistry / Q000378:metabolism*; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism*; D054645:Protein Phosphatase 1; D011817:Rabbits; D012694:Serine / Q000378:metabolism
D012694:Serine; D011494:Protein Kinases; D047388:Casein Kinases; D010749:Phosphoprotein Phosphatases; D054645:Protein Phosphatase 1