Inhibition of catalytic unit of adenylate cyclase and activation of GTPase of Ni protein by beta gamma-subunits of GTP-binding proteins.

Abstract:

:A protein factor which inhibited adenylate cyclase was purified to apparent homogeneity from rat brain and identified as the beta gamma-subunits of the GTP-binding regulatory proteins of adenylate cyclase. (i) The beta gamma-subunits (protein factor) inhibited the partially purified catalytic unit of adenylate cyclase in the presence of an activator, forskolin or the stimulative regulatory protein (Ns), to 60 and 40% of the control, respectively; inhibition of the catalytic unit in the presence of forskolin required no guanine nucleotides. (ii) The subunits enhanced the GTPase activity of the purified alpha-subunit of the inhibitory regulatory protein (Ni alpha) 3.8-fold. (iii) The subunits stimulated ADP-ribosylation of Ni alpha catalyzed by islet-activating protein (pertussis toxin). ADP-ribosylation had no effect on the GTPase activity of Ni alpha in the presence of the beta gamma-subunits. The results suggest that direct inhibition of the catalytic unit by the beta gamma-subunits liberated from Ni is essential for the receptor-mediated inhibition of adenylate cyclase.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Enomoto K,Asakawa T

doi

10.1016/0014-5793(86)80650-0

subject

Has Abstract

pub_date

1986-06-23 00:00:00

pages

63-8

issue

1

eissn

0014-5793

issn

1873-3468

pii

0014-5793(86)80650-0

journal_volume

202

pub_type

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