Regulation of polyphosphoinositide-specific phospholipase C activity by purified Gq

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

Research output: Contribution to journalArticle

667 Scopus citations

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-diacyglycerol. 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 α 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.

Original languageEnglish (US)
Pages (from-to)804-807
Number of pages4
JournalScience
Volume251
Issue number4995
DOIs
StatePublished - Jan 1 1991

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