Gi/o Protein-Dependent and -Independent Actions of Pertussis Toxin (PTX)

Abstract

Pertussis toxin (PTX) is a typical A-B toxin. The A-protomer (S1 subunit) exhibits ADP-ribosyltransferase activity. The B-oligomer consists of four subunits (S2 to S5) and binds extracellular molecules that allow the toxin to enter the cells. The A-protomer ADP-ribosylates the α subunits of heterotrimeric Gi/o proteins, resulting in the receptors being uncoupled from the Gi/o proteins. The B-oligomer binds proteins expressed on the cell surface, such as Toll-like receptor 4, and activates an intracellular signal transduction cascade. Thus, PTX modifies cellular responses by at least two different signaling pathways; ADP-ribosylation of the Gαi/o proteins by the A-protomer (Gi/o protein-dependent action) and the interaction of the B-oligomer with cell surface proteins (Gi/o protein-independent action).

Keywords

• A-protomer
• ADP-ribosylation
• B-oligomer
• Gi/o-dependent
• Gi/o-independent
• heterotrimeric G protein
• G protein-coupled receptor
• pertussis toxin
• Toll-like receptor 4