Activation of adenylate cyclase by the diterpene forskolin does not require the guanine nucleotide regulatory protein.
Forskolin, a novel diterpene activator of adenylate cyclase in membranes and intact cells, activates the enzyme in membranes from mutant cyc-S49 murine lymphoma cells and the soluble enzyme from rat testes. Each of these enzymes consists only of the catalytic subunit and does not have a functional guanine nucleotide-binding protein. In both cases forskolin converts the manganese-dependent enzymes to a form which does not require manganese for activity. Forskolin can also stimulate a detergent-solubilized preparation of adenylate cyclase from rat cerebral cortex. Activation of adenylate cyclase by forskolin is therefore not dependent on a perturbation of membrane structure nor does it require a functional guanine nucleotide-binding subunit.
D000262:Adenylyl Cyclases / Q000378:metabolism*; D000818:Animals; D002460:Cell Line; D002462:Cell Membrane / Q000201:enzymology; D005576:Colforsin; D004224:Diterpenes / Q000494:pharmacology*; D004789:Enzyme Activation; D019204:GTP-Binding Proteins; D006165:Guanylyl Imidodiphosphate / Q000494:pharmacology; D007545:Isoproterenol / Q000494:pharmacology; D007700:Kinetics; D008223:Lymphoma; D008345:Manganese / Q000494:pharmacology; D051379:Mice; D009374:Neoplasms, Experimental; D011956:Receptors, Cell Surface / Q000502:physiology*; D012969:Sodium Fluoride / Q000494:pharmacology
D004224:Diterpenes; D011956:Receptors, Cell Surface; D005576:Colforsin; D006165:Guanylyl Imidodiphosphate; D008345:Manganese; D012969:Sodium Fluoride; D019204:GTP-Binding Proteins; D000262:Adenylyl Cyclases; D007545:Isoproterenol