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

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 eff...

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Bibliographic Details
Published in:FEBS letters 1985-08, Vol.188 (1), p.150-154
Main Authors: Skurat, Alexander V., Yurkova, Maria S., Khropov, Yuri V., Bulargina, Tamara V., Severin, Eugene S.
Format: Article
Language:English
Subjects:
Adenylate cyclase
Caudate nucleus
Forskolin
GTP 2',3'-dialdehyde
N s,protein
Reconstitution
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Summary: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 s protein. Such modification leads to the elimination of the N s-mediated regulation of the enzyme.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(85)80893-0