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
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
收藏
页码:121 / 124
页数:4
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