REGULATION OF POLYPHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE-C ACTIVITY BY PURIFIED GQ

被引：850

作者：

SMRCKA, AV ^{[1
]}

HEPLER, JR ^{[1
]}

BROWN, KO ^{[1
]}

STERNWEIS, PC ^{[1
]}

机构：

[1] UNIV TEXAS,SW MED CTR,DEPT PHARMACOL,DALLAS,TX 75235

来源：

SCIENCE | 1991年 / 251卷 / 4995期

关键词：

D O I：

10.1126/science.1846707

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The hydrolysis of phosphatidylinositol 4,5-bisphosphate (PIP2) by phospholipase C yields the second messengers inositol 1,4,5-trisphosphate (InsP3) and 1,2-diacylglycerol. This activity is regulated by a variety of hormones through G protein pathways. However, the specific G protein or proteins involved has not been identified. The alpha-subunit of a newly discovered pertussis toxin-insensitive G protein (G(q)) has recently been isolated and is now shown to stimulate the activity of polyphosphoinositide-specific phospholipase C (PI-PLC) from bovine brain. Both the maximal activity and the affinity of PI-PLC for calcium ion were affected. These results identify G(q) as a G protein that regulates PI-PLC.

引用

页码：804 / 807

页数：4

共 34 条

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