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Toxins 2010, 2(2), 205-214; doi:10.3390/toxins2020205

Pasteurella multocida Toxin Activates Various Heterotrimeric G Proteins by Deamidation

Institute for Experimental and Clinical Pharmacology and Toxicology, University of Freiburg, 79104 Freiburg, Germany
* Author to whom correspondence should be addressed.
Received: 24 November 2009 / Revised: 19 January 2010 / Accepted: 27 January 2010 / Published: 28 January 2010
(This article belongs to the Special Issue Bacterial Protein Toxins)
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Pasteurella multocida produces a 146-kDa protein toxin (Pasteurella multocida toxin, PMT), which stimulates diverse cellular signal transduction pathways by activating heterotrimeric G proteins. PMT deamidates a conserved glutamine residue of the α-subunit of heterotrimeric G proteins that is essential for GTP-hydrolysis, thereby arresting the G protein in the active state. The toxin substrates are Gαq13 and the Gαi-family proteins. Activation of these α-subunits causes stimulation of phospholipase Cβ, Rho-guanine nucleotide exchange factors or inhibition of adenylyl cyclase. This article provides the current knowledge on PMT concerning the structure-function analysis based on the crystal structure and recently elucidated molecular mode of action. Furthermore, the impact of PMT on cellular signaling is discussed.
Keywords: G protein; α-subunit; deamidation; GTPase; Gαq; Gαi; Gα12/13 G protein; α-subunit; deamidation; GTPase; q; i; 12/13
This is an open access article distributed under the Creative Commons Attribution License (CC BY) which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Orth, J.H.C.; Aktories, K. Pasteurella multocida Toxin Activates Various Heterotrimeric G Proteins by Deamidation. Toxins 2010, 2, 205-214.

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