Publication: G<inf>i/o</inf> protein-dependent and -independent actions of pertussis toxin (ptx)
Issued Date
2011-07-01
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ISSN
20726651
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2-s2.0-79960756461
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Mahidol University
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SCOPUS
Bibliographic Citation
Toxins. Vol.3, No.7 (2011), 884-899
Suggested Citation
Supachoke Mangmool, Hitoshi Kurose G<inf>i/o</inf> protein-dependent and -independent actions of pertussis toxin (ptx). Toxins. Vol.3, No.7 (2011), 884-899. doi:10.3390/toxins3070884 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/11920
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Title
G<inf>i/o</inf> protein-dependent and -independent actions of pertussis toxin (ptx)
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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 G i/o proteins, resulting in the receptors being uncoupled from the G i/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 Gα i/o proteins by the A-protomer (G i/o protein-dependent action) and the interaction of the B-oligomer with cell surface proteins (G i/o protein-independent action). © 2011 by the authors; licensee MDPI, Basel, Switzerland.