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J. Biol. Chem., Vol. 256, Issue 19, 9799-9801, Oct, 1981
K Seamon and JW Daly
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.
Activation of adenylate cyclase by the diterpene forskolin does not require the guanine nucleotide regulatory protein
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