Toxins 2011, 3(7), 884-899; doi:10.3390/toxins3070884

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

1email and 2,* email
Received: 13 April 2011; in revised form: 14 June 2011 / Accepted: 16 June 2011 / Published: 15 July 2011
(This article belongs to the Special Issue Novel Properties of Well-Characterized Toxins)
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
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
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MDPI and ACS Style

Mangmool, S.; Kurose, H. Gi/o Protein-Dependent and -Independent Actions of Pertussis Toxin (PTX). Toxins 2011, 3, 884-899.

AMA Style

Mangmool S, Kurose H. Gi/o Protein-Dependent and -Independent Actions of Pertussis Toxin (PTX). Toxins. 2011; 3(7):884-899.

Chicago/Turabian Style

Mangmool, Supachoke; Kurose, Hitoshi. 2011. "Gi/o Protein-Dependent and -Independent Actions of Pertussis Toxin (PTX)." Toxins 3, no. 7: 884-899.

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