PHOSPHORYLATION OF CALCINEURIN - EFFECT ON CALMODULIN BINDING

被引：13

作者：

CALALB, MB ^{[1
]}

KINCAID, RL ^{[1
]}

SODERLING, TR ^{[1
]}

机构：

[1] NIAAA,PHYSIOL & PHARMACOL STUDIES LAB,IMMUNOL SECT,ROCKVILLE,MD 20854

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1990年 / 172卷 / 02期

关键词：

D O I：

10.1016/0006-291X(90)90708-U

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 effect of phosphorylation of calcineurin on calmodulin (CaM) binding was examined using a synthetic peptide which contains the CaM-binding domain and the serine phosphorylation site. The peptide, corresponding to residues 391-414 of brain calcineurin A subunit, was rapidly phosphorylated by protein kinase C and Ca2+ CaM-dependent protein kinase II but not by cAMP-dependent protein kinase. Phosphorylation of peptide 391-414 did not significantly alter the binding of CaM when compared to the non-phosphorylated peptide. © 1990.

引用

页码：551 / 556

页数：6

共 18 条

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