PHOSPHORYLATION OF GI PROTEIN BY CYCLIC AMP-DEPENDENT PROTEIN-KINASE INHIBITS ITS DISSOCIATION INTO ALPHA-SUBUNITS AND BETA-GAMMA-SUBUNITS BY MG2+ AND GTP-GAMMA-S

被引：22

作者：

IMAIZUMI, T ^{[1
]}

WATANABE, Y ^{[1
]}

YOSHIDA, H ^{[1
]}

机构：

[1] OSAKA UNIV,SCH MED,DEPT PHARMACOL 1,2-2 YAMADAOKA,SUITA,OSAKA 565,JAPAN

来源：

EUROPEAN JOURNAL OF PHARMACOLOGY-MOLECULAR PHARMACOLOGY SECTION | 1991年 / 207卷 / 03期

关键词：

GTP-BINDING PROTEIN (INHIBITORY); GI PROTEIN; PERTUSSIS TOXIN; ADP-RIBOSYLATION; PHOSPHORYLATION; CYCLIC AMP-DEPENDENT PROTEIN KINASE;

D O I：

10.1016/0922-4106(91)90030-L

中图分类号：

R9 [药学];

学科分类号：

1007 ;

摘要：

Pretreatment of partially purified inhibitory GTP-binding protein (G(i), 41 kDa) with activated cyclic AMP-dependent protein kinase (PKA) decreases its ADP-ribosylation by islet-activating protein (pertussis toxin, IAP). We examined whether this decrease was associated with dissociation of the trimer of alpha-beta-gamma-subunits of G(i) protein into alpha-subunits and beta-gamma-subunits. Results showed that phosphorylation of the G(i) protein by PKA impaired its dissociation into alpha-subunits and beta-gamma-subunits by 50 mM Mg2+ and 100-mu-M GTP-gamma-S. The results suggested that phosphorylation of the G(i) protein by PKA possibly caused a conformational change of the trimer G(i) protein.

引用

页码：189 / 194

页数：6

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