guanosine-triphosphate has been researched along with catechol* in 1 studies
1 other study(ies) available for guanosine-triphosphate and catechol
| Article | Year |
|---|---|
Phospholipase C-beta 1 is a GTPase-activating protein for Gq/11, its physiologic regulator.
Purified M1 muscarinic cholinergic receptor and Gq/11 were coreconstituted in lipid vesicles. Addition of purified phospholipase C-beta 1 (PLC-beta 1) further stimulated the receptor-promoted steady-state GTPase activity of Gq/11 up to 20-fold. Stimulation depended upon receptor-mediated GTP-GDP exchange. Addition of PLC-beta 1 caused a rapid burst of hydrolysis of Gq/11-bound GTP that was at least 50-fold faster than in its absence. Thus, PLC-beta 1 stimulates hydrolysis of Gq/11-bound GTP and acts as a GTPase-activating protein (GAP) for its physiologic regulator, Gq/11. GTPase-stimulating activity was specific both for PLC-beta 1 and Gq/11. Such GAP activity by an effector coupled to a trimeric G protein can reconcile slow GTP hydrolysis by pure G proteins in vitro with fast physiologic deactivation of G protein-mediated signaling. Topics: Animals; Atropine; Catechols; Enzyme Activation; GTP Phosphohydrolases; GTP-Binding Proteins; GTPase-Activating Proteins; Guanosine Diphosphate; Guanosine Triphosphate; Humans; Hydrolysis; Kinetics; Proteins; Receptors, Adrenergic, beta; Receptors, Muscarinic; Turkeys; Type C Phospholipases | 1992 |