title: Pasteurella multocida toxin activates various heterotrimeric G proteins by deamidation.
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 Gα(q) Gα(13) 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.
authors: Institute for Experimental and Clinical Pharmacology and Toxicology, University of Freiburg, 79104 Freiburg, Germany. Joachim.Orth@pharmakol.uni-freiburg.de
authors: Joachim H C
authors: JH
authors: Orth
authors: Klaus
authors: K
authors: Aktories
mesh_terms: D020962:Heterotrimeric GTP-Binding Proteins; D016979:Pasteurella multocida / Q000378:metabolism; D015398:Signal Transduction
chemical_list: D020962:Heterotrimeric GTP-Binding Proteins