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

作者信息

Agostinis P, Marin O, James P, Hendrix P, Merlevede W, Vandenheede J R, Pinna L A

机构信息

Afdeling Biochemie, Faculteit Geneeskunde, Katholieke Universiteit te Leuven, Belgium.

出版信息

FEBS Lett. 1992 Jun 29;305(2):121-4. doi: 10.1016/0014-5793(92)80877-j.

DOI:10.1016/0014-5793(92)80877-j
PMID:1319929
Abstract

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.

摘要

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