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

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

1
 and
2,*
1 Department of Pharmacology, Faculty of Pharmacy, Mahidol University, 447 Sri-Ayudhaya, Rajathevi, Bangkok 10400, Thailand 2 Department of Pharmacology and Toxicology, Graduate School of Pharmaceutical Sciences, Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka 812-8582, Japan
* Author to whom correspondence should be addressed.
Received: 13 April 2011 / Revised: 14 June 2011 / Accepted: 16 June 2011 / Published: 15 July 2011
(This article belongs to the Special Issue Novel Properties of Well-Characterized Toxins)
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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 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
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).
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Mangmool, S.; Kurose, H. Gi/o Protein-Dependent and -Independent Actions of Pertussis Toxin (PTX). Toxins 2011, 3, 884-899.

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