Interaction of mastoparan with the low molecular mass GTP‐binding proteins rho/rac
Gertrud Koch, Barbara Haberman, Christiane Mohr, Ingo Just, Klaus Aktories
Abstract
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Gertrud Koch, Barbara Haberman, Christiane Mohr, Ingo Just, Klaus Aktories
Abstract
Open-access reader
Mastoparan, which has been shown to active G proteins, inhibits the ADP-ribosylation of 20 kDa human platelet membrane proteins catalyzed by Clostridium botulinum exoenzyme C3 half-maximally and maximally (90%) at 20 and 100 microM concentrations, respectively. Inhibition of ADP-ribosylation was enhanced by GTP-gamma S. Mastoparan increased GTP hydrolysis by porcine brain rho protein and stimulated GTP binding in a concentration dependent manner. The data suggest that mastoparan not only interacts with heterotrimeric G proteins but also with low molecular mass GTP-binding proteins of the rho/rac family.
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Mastoparan, which has been shown to active G proteins, inhibits the ADP-ribosylation of 20 kDa human platelet membrane proteins catalyzed by Clostridium botulinum exoenzyme C3 half-maximally and maximally (90%) at 20 and 100 microM concentrations, respectively. Inhibition of ADP-ribosylation was enhanced by GTP-gamma S. Mastoparan increased GTP hydrolysis by porcine brain rho protein and stimulated GTP binding in a concentration dependent manner. The data suggest that mastoparan not only interacts with heterotrimeric G proteins but also with low molecular mass GTP-binding proteins of the rho/rac family.
Key concepts: Mastoparan, Heterotrimeric G protein, GTP', G protein, Chemistry, GTP-binding protein regulators, Biochemistry, ADP-ribosylation