PROTEIN PHOSPHATASE-ACTIVITY IN ACETYLCHOLINE RECEPTOR-ENRICHED MEMBRANES

被引：38

作者：

GORDON, AS ^{[1
]}

MILFAY, D ^{[1
]}

DAVIS, CG ^{[1
]}

DIAMOND, I ^{[1
]}

机构：

[1] UNIV CALIF SAN FRANCISCO,SCH MED,DEPT PEDIAT,SAN FRANCISCO,CA 94143

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1979年 / 87卷 / 03期

关键词：

D O I：

10.1016/0006-291X(79)92039-4

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：

Phosphorylation of the acetylcholine receptor (AChR)* * Abbreviation: AChR, acetylcholine receptor; EGTA, ethyleneglycolbis (β-aminoethyl ether)-N, N1-tetraacetic acid; DTT, dithiothreitol has been demonstrated in AChR-enriched membranes prepared from the electric organ of Torpedo californica. In this report we show that the same AChR-enriched membrane fraction also contains phosphoprotein phosphatase activity which dephosphorylates both the endogenous AChR and exogenous phosphorylated casein. Release of [32P] PO4 from phosphorylated casein was shown to be inhibited by F- as well as GTP. cAMP and cGMP were without effect. Dephosphorylation of the membrane-bound AChR was also inhibited by F-. This phosphorylation-dephosphorylation mechanism may play a role in mediating the function of the AChR at the synapse. © 1979.

引用

页码：876 / 883

页数：8

共 8 条

[1]

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