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Toxins 2010, 2(2), 205-214; doi:10.3390/toxins2020205
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Pasteurella multocida Toxin Activates Various Heterotrimeric G Proteins by Deamidation

 and
*
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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Abstract

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 3.0).
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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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