PHOSPHORYLATION BY PROTEIN KINASE-C OF THE MUSCARINIC ACETYLCHOLINE-RECEPTOR

被引：46

作者：

HAGA, K ^{[1
]}

HAGA, T ^{[1
]}

ICHIYAMA, A ^{[1
]}

机构：

[1] HAMAMATSU UNIV SCH MED, DEPT BIOCHEM, HAMAMATSU, SHIZUOKA 43131, JAPAN

来源：

JOURNAL OF NEUROCHEMISTRY | 1990年 / 54卷 / 05期

关键词：

Muscarinic receptor‐Acetylcholine receptor; Phosphorylation; Protein kinase C;

D O I：

10.1111/j.1471-4159.1990.tb01216.x

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：

Abstract: Muscarinic acetylcholine receptors purified from porcine cerebrum were phosphorylated by protein kinase C purified from the same tissue. More than 1 mol of phosphate was incorporated per mole of receptor, with both serine and threonine residues being phosphorylated. Neither the degree nor the rate of the phosphorylation was affected by the presence or absence of acetylcholine. GTP‐sensitive high‐affinity binding with acetylcholine was observed for muscarinic receptors reconstituted with GTP‐binding proteins (Gi or Go), irrespective of whether muscarinic receptors or the GTP‐binding proteins had been phosphorylated by protein kinase C or not. This indicates that the interaction between purified muscarinic receptors and purified GTP‐binding proteins in vitro is not affected by their phosphorylation. Copyright © 1990, Wiley Blackwell. All rights reserved

引用

页码：1639 / 1644

页数：6

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