Introduction
Phospholipase C (PLC) catalyzes the hydrolysis of phosphatidylinositol 4,5-bisphosphate [IP2] to the second messengers inositol 1,4,5-trisphosphate [IP3] and diacylglycerol [DAG] in an essential step for the physiological action of many hormones, neurotransmitters, growth factors, and other extracellular stimuli. These cascades use signaling complexes consisting of G alpha subunits of the Gq family of heterotrimeric guanine nucleotide–binding proteins (G proteins) and PLC-beta isozymes (β1-4). Agonist-stimulated receptors increase exchange of guanosine diphosphate (GDP) for guanosine triphosphate (GTP) on Gαq. GTP-bound Gαq engages and activates PLC- β3, and PLC- β3 increases up to three orders of magnitude the rate of hydrolysis of GTP by its activating G protein. This is a unique mechanism when the PLC-β3 enzyme has the ability to terminate the Gαq protein signal in addition to being activated by it.[1] [2]
Structural highlights
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