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J. Biol. Chem., Vol. 263, Issue 14, 6491-6494, May, 1988
T Higashijima, S Uzu, T Nakajima and EM Ross
Mastoparan, a peptide toxin from wasp venom, is a nonspecific secretagogue.
We show here that mastoparan increases the GTPase activity and the rate of
nucleotide binding of several purified GTP- binding regulatory proteins (G
proteins) whose function is to couple cell-surface receptors to
intracellular mediators. Mastoparan accelerated
guanosine-5'-(3-O-thiotriphosphate binding and consequent G protein
activation in part by promoting the dissociation of bound GDP, the
mechanism by which receptors regulate G proteins. ADP-ribosylation by
pertussis toxin, which uncouples receptors from G proteins, selectively
inhibited mastoparan-stimulated activation. Like receptors, mastoparan was
more potent if the G protein was reconstituted in phospholipid vesicles and
was active at micromolar concentrations of Mg2+. The structure of
mastoparan in a lipid bilayer is similar to that predicted for a cationic
intracellular loop of G protein-coupled receptors. Mastoparan thus displays
a novel mode of toxicity by acting directly on G proteins to mimic the role
normally played by agonist- liganded receptors.
Mastoparan, a peptide toxin from wasp venom, mimics receptors by activating GTP-binding regulatory proteins (G proteins)
Department of Pharmacology, Southwestern Graduate School of Biomedical Sciences, University of Texas Health Science Center, Dallas 75235-9041.
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