GTP-preferring protein phosphorylation systems in brain membranes: Possible role in adenylate cyclase regulation

Ehrlich, Yigal H.; Whittemore, Scott R.; Lambert, Roger; Ellis, John E.; Graber, Stephen G.; Lenox, Robert H.

doi:10.1016/0006-291x(82)91547-9

Cited by 8 publications

(1 citation statement)

References 15 publications

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“…It has been suggested that phosphorylation/dephosphorylation cycles may regulate adenylate cyclase activity (9,23,29). Homologous desensitization in the frog-erythrocyte has been linked to phosphorylation of the beta-adrenergic receptor (26).…”

Section: Discussionmentioning

confidence: 99%

GTP-independent stimulation of rabbit heart adenylate cyclase by isoproterenol at physiological ATP concentrations

1989

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Isoproterenol increased the activity of the adenylate cyclase of rabbit heart sarcolemmal membranes in the absence of added GTP. ATP, the ATP-regenerating system, and the sarcolemmal membrane preparation were eliminated as possible sources of contaminating GTP. Isoproterenol-stimulation increased as ATP was raised. At 0.5 mM ATP, isoproterenol increased activity by 19% whereas at 5 mM ATP isoproterenol increased activity by 121%. There was no change in basal activity between 0.5 and 5 mM ATP. Stimulation by Gpp(NH)p and NaF increased slightly between 0.5 and 5 mM ATP; stimulation by KCl was unaffected. GTP does not activate cyclase d. GTP does not activate cyclase to the same extent as Gpp(NH)p even though the two act at the same site on Ns (the stimulatory guanine nucleotide-binding protein). GTP decreased cyclase activation by Gpp(NH)p in a concentration-dependent fashion when the two were added to the assay simultaneously. Increasing ATP from 0.5 to 5 mM did not reduce activation by Gpp(NH)p when both were added simultaneously to the assay. This suggests that ATP does not interact with the same site as Gpp(NH)p. ATP gamma S, an analogue of ATP which irreversibly thiophosphorylates proteins, did not irreversibly support activation by isoproterenol. The effect of ATP in supporting isoproterenol stimulation is not, therefore, thought to be due to phosphorylation of a protein.

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Section: Discussionmentioning

confidence: 99%