PHOSPHORYLATION OF THE PHOSPHATASE MODULATOR SUBUNIT (INHIBITOR-2) BY CASEIN KINASE-1 - IDENTIFICATION OF THE PHOSPHORYLATION SITES

被引：25

作者：

AGOSTINIS, P

MARIN, O

JAMES, P

HENDRIX, P

MERLEVEDE, W

VANDENHEEDE, JR

PINNA, LA

机构：

[1] CATHOLIC UNIV LEUVEN,FAC GENEESKUNDE,AFDELING BIOCHEM,CAMPUS GASTHUISBERG,B-3000 LOUVAIN,BELGIUM

[2] UNIV PADUA,DIPARTIMENTO CHIM BIOL,I-35100 PADUA,ITALY

[3] SWISS FED INST TECHNOL,PROT CHEM SERV,CH-8092 ZURICH,SWITZERLAND

[4] SWISS FED INST TECHNOL,FORSCHUNGSLAB,CH-8092 ZURICH,SWITZERLAND

来源：

FEBS LETTERS | 1992年 / 305卷 / 02期

关键词：

PHOSPHATASE MODULATOR; INHIBITOR-2; CASEIN KINASE-1; CASEIN KINASE-2; PHOSPHORYLATION SITE;

D O I：

10.1016/0014-5793(92)80877-J

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：121 / 124

页数：4

共 21 条

[1] PHOSPHORYLATION OF THE MODULATOR PROTEIN OF THE ATP,MG-DEPENDENT PROTEIN PHOSPHATASE BY CASEIN KINASE-TS - REVERSAL BY PCS PHOSPHATASES AND CONTROL BY DISTINCT PHOSPHORYLATION SITE(S) [J].