Interaction of GTP-binding proteins with calmodulin.
Two GTP-binding proteins (Gi and Go), which were the substrates for islet-activating protein, pertussis toxin, were purified from bovine cerebral cortical membranes. Both Gi and Go completely inhibited calmodulin-stimulated cyclic nucleotide phosphodiesterase activity. The same concentrations of these proteins, however, had no appreciable effect on the basal phosphodiesterase activity. The isolated Gi alpha and beta gamma subunits of GTP-binding proteins were potent inhibitors of the calmodulin-stimulated phosphodiesterase activity, but Go alpha was very weak. Therefore, the beta gamma subunits were likely to be the major active molecules in the brain membranes. GTP-binding proteins were shown to bind directly to calmodulin in a Ca2+-dependent manner by a gel permeation binding experiment.
D015087:2',3'-Cyclic-Nucleotide Phosphodiesterases / Q000037:antagonists & inhibitors; D000818:Animals; D002147:Calmodulin / Q000378:metabolism*; D002417:Cattle; D002540:Cerebral Cortex / Q000201:enzymology; D019204:GTP-Binding Proteins / Q000378:metabolism*; D066298:In Vitro Techniques; D008297:Male; D051381:Rats; D013737:Testis / Q000378:metabolism
D002147:Calmodulin; D015087:2',3'-Cyclic-Nucleotide Phosphodiesterases; D019204:GTP-Binding Proteins