Regulation of polyphosphoinositide-specific phospholipase C activity by purified Gq

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

doi:10.1126/science.1846707

Regulation of polyphosphoinositide-specific phospholipase C activity by purified G_q

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

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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 (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.

Original language	English (US)
Pages (from-to)	804-807
Number of pages	4
Journal	Science
Volume	251
Issue number	4995
DOIs	https://doi.org/10.1126/science.1846707
State	Published - 1991

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title = "Regulation of polyphosphoinositide-specific phospholipase C activity by purified Gq",

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.",

author = "Smrcka, {Alan V.} and Hepler, {John R.} and Brown, {Kendall O.} and Sternweis, {Paul C.}",

year = "1991",

doi = "10.1126/science.1846707",

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T1 - Regulation of polyphosphoinositide-specific phospholipase C activity by purified Gq

AU - Smrcka, Alan V.

AU - Hepler, John R.

AU - Brown, Kendall O.

AU - Sternweis, Paul C.

PY - 1991

Y1 - 1991

N2 - 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.

AB - 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.

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Regulation of polyphosphoinositide-specific phospholipase C activity by purified G_q

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