2',3'-Dialdehyde of GTP blocks regulatory functions of adenylate cyclase N sprotein

Autor: Skurat, Alexander V., Yurkova, Maria S., Khropov, Yuri V., Bulargina, Tamara V., Severin, Eugene S.
Zdroj: FEBS Letters; January 1985, Vol. 188 Issue: 1 p150-154, 5p
Abstrakt: Preincubation of bovine caudate nucleus membranes with the 2',3'-dialdehyde of GTP (oGTP) reduces adenylate cyclase activation by guanylyl imidodiphosphate (GppNHp) in a time-dependent fashion. A slower rate of inhibition is observed if membranes are treated with both GTP and oGTP. The efficacy of oGTP action is enhanced by raising the Mg 2+concentration. Reduction of adenylate cyclase sensitivity to GppNHp is followed by an irreversible decrease of enzyme stimulation by forskolin. Addition of a Lubrol soluble preparation from guinea pig lung membranes to oGTP-treated caudate nucleus membranes causes restoration of the adenylate cyclase sensitivity to GppNHp. These data suggest that oGTP blocks the GTP-binding site of the adenylate cyclase system localized on the N sprotein. Such modification leads to the elimination of the N s-mediated regulation of the enzyme.
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