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

Pasteurella multocida Toxin Activates Various Heterotrimeric G Proteins by Deamidation

 and *
Received: 24 November 2009; in revised form: 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 which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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MDPI and ACS Style

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

AMA Style

Orth JHC, Aktories K. Pasteurella multocida Toxin Activates Various Heterotrimeric G Proteins by Deamidation. Toxins. 2010; 2(2):205-214.

Chicago/Turabian Style

Orth, Joachim H. C.; Aktories, Klaus. 2010. "Pasteurella multocida Toxin Activates Various Heterotrimeric G Proteins by Deamidation." Toxins 2, no. 2: 205-214.


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