pasteurella multocida toxin activates various heterotrimeric g proteins by deamidation巴斯德菌multocida毒素激活各种heterotrimeric g蛋白脱酰氨基作用.pdfVIP

pasteurella multocida toxin activates various heterotrimeric g proteins by deamidation巴斯德菌multocida毒素激活各种heterotrimeric g蛋白脱酰氨基作用.pdf

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pasteurella multocida toxin activates various heterotrimeric g proteins by deamidation巴斯德菌multocida毒素激活各种heterotrimeric g蛋白脱酰氨基作用

Toxins 2010, 2, 205-214; doi:10.3390/toxins2020205 OPEN ACCESS toxins ISSN 2072-6651 /journal/toxins Review Pasteurella multocida Toxin Activates Various Heterotrimeric G Proteins by Deamidation Joachim H. C. Orth and Klaus Aktories * Institute for Experimental and Clinical Pharmacology and Toxicology, University of Freiburg, 79104 Freiburg, Germany; E-Mail: Joachim.Orth@pharmakol.uni-freiburg.de * Author to whom correspondence should be addressed; E-Mail: Klaus.Aktories@pharmakol.uni-freiburg.de; Tel.: +49-761-203-5301; Fax: +49-761-203-5311. Received: 24 November 2009; in revised form: 19 January 2010 / Accepted: 27 January 2010 / Published: 28 January 2010 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 Gα and the Gα-family proteins. q 13 i 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 rece

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