Pasteurella multocida Toxin Activates Various Heterotrimeric G Proteins by Deamidation

Toxins

Joachim H. C. Orth¹ 

[1] Institute for Experimental and Clinical Pharmacology and Toxicology, University of Freiburg, 79104 Freiburg, Germany;

关键词: G protein;    α-subunit;    deamidation;    GTPase;    Gα_q;    Gα_i;    Gα_12/13;   

DOI  :  10.3390/toxins2020205

来源: mdpi

【 摘 要 】

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 Gα_q Gα₁₃ and the Gα_i-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.

【 授权许可】

CC BY   
© 2010 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland