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

Alexander V. Skurat, Maria S. Yurkova, Yuri V. Khropov, Tamara V. Bulargina, Eugene S. Severin

Research output: Contribution to journalArticle

4 Scopus citations


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 Mg2+ 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 Ns protein. Such modification leads to the elimination of the Ns-mediated regulation of the enzyme.

Original languageEnglish (US)
Pages (from-to)150-154
Number of pages5
JournalFEBS Letters
Issue number1
StatePublished - Aug 19 1985
Externally publishedYes


  • Adenylate cyclase
  • Caudate nucleus
  • Forskolin
  • GTP 2',3'-dialdehyde
  • N,protein
  • Reconstitution

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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