Phosphorylation of the phosphatase modulator subunit (inhibitor‐2) by casein kinase‐1 Identification of the phosphorylation sites

FEBS Letters

Merlevede, Wilfried¹  Vandenheede, Jackie R.¹  James, Peter²  Pinna, Lorenzo A.³  Agostinis, Patrizia¹  Marin, Oriano³  Hendrix, Peter¹ 

[1] Afdeling Biochemie, Faculteit Geneeskunde, Katholieke Universiteit te Leuven, Leuven, Belgium;Proteinchemie, Service und Forschungslabor, ETH Zentrum, Zürich, Switzerland;Dipartimento di Chimica Biologica, Universitá di Padova, Padova, Italy

关键词: Phosphatase modulator;    Inhibitor-2;    Casein kinase-1;    Casein kinase-2;    Phosphorylation site;    CK-1;    casein kinase-1;    CK-2;    casein kinase-2;    kinase FA/GSK3;    kinase FA/glycogen synthase kinase 3;    M;    modulator subunit;    (FcM);    inactive ATP;    Mg-dependent protein phosphatase (protein phosphatase II);    PTH;    phenylthiohydantoin;    PTC;    phenylthiocarbamoyl;   

DOI  :  10.1016/0014-5793(92)80877-J

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The isolated modulator subunit of the inactive protein phosphatase-1 is phosphorylated in vitro by casein kinase-1 at two different site 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.

【 授权许可】

Unknown