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    Science. 1991 Feb 15;251(4995):804-7.

    Regulation of polyphosphoinositide-specific phospholipase C activity by purified Gq.

    Smrcka AV, Hepler JR, Brown KO, Sternweis PC.

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    Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas 75235.

    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.

    PMID:
    1846707
    [PubMed - indexed for MEDLINE]

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