1991•ScienceRequires access

Regulation of Polyphosphoinositide-specific Phospholipase C Activity by Purified G q

Alan V. Smrcka, John R. Hepler, Kendall O. Brown, Paul C. Sternweis

Abstract

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 (Gq) 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 Gq as a G protein that regulates PI-PLC.

About this research paper

What this paper is about

Why it matters

OpenAlex reports 904 citations for this work. Citation counts describe recorded attention and do not establish research quality.

Key contribution

A contribution statement is not available in the OpenAlex record.

Method / approach

Method details are not available in the OpenAlex metadata.

Main findings

Findings are not separately available in the OpenAlex metadata.

Limitations

Limitations are not available in the OpenAlex metadata.

Applications

Application details are not available in the OpenAlex metadata.

Available abstract

Key concepts: Gq alpha subunit, Phospholipase C, Second messenger system, G protein, Phosphoinositide phospholipase C, Diacylglycerol kinase, Pertussis toxin, Phosphatidylinositol