Regulation of polyphosphoinositide-specific phospholipase C activity by purified Gq

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 invo...

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Veröffentlicht in:	Science (American Association for the Advancement of Science) 1991-02, Vol.251 (4995), p.804-807
Hauptverfasser:	SMRCKA, A. V, HEPLER, J. R, BROWN, K. O, STERNWEIS, P. C
Format:	Artikel
Sprache:	eng
Schlagworte:	Aluminum - pharmacology Aluminum Compounds Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Calcium - physiology Cattle Cell regulation Cellular control mechanisms Enzyme Activation - drug effects Enzymes and enzyme inhibitors Fluorides - pharmacology Fundamental and applied biological sciences. Psychology G proteins GTP-Binding Proteins - drug effects GTP-Binding Proteins - physiology Guanosine Diphosphate Hydrolases In Vitro Techniques Phosphatidylinositol Phosphatidylinositol Diacylglycerol-Lyase Phosphatidylinositols Phosphoinositide Phospholipase C Phosphoinositides Phospholipases Phosphoric Diester Hydrolases - metabolism Substrate Specificity
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Zusammenfassung:	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.
ISSN:	0036-8075 1095-9203
DOI:	10.1126/science.1846707