Linked Life Data

22069582

Source:http://linkedlifedata.com/resource/pubmed/id/22069582

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2011-11-9
pubmed:abstractText
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 ?-subunit of heterotrimeric G proteins that is essential for GTP-hydrolysis, thereby arresting the G protein in the active state. The toxin substrates are G?(q) G?(13) and the G?(i)-family proteins. Activation of these ?-subunits causes stimulation of phospholipase C?, 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.
pubmed:language
eng
pubmed:journal
pubmed:status
PubMed-not-MEDLINE
pubmed:month
Feb
pubmed:issn
2072-6651
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
2
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
205-14
pubmed:dateRevised
2011-11-14
pubmed:year
2010
pubmed:articleTitle
Pasteurella multocida Toxin Activates Various Heterotrimeric G Proteins by Deamidation.
pubmed:affiliation
Institute for Experimental and Clinical Pharmacology and Toxicology, University of Freiburg, 79104 Freiburg, Germany; Email: Joachim.Orth@pharmakol.uni-freiburg.de.
pubmed:publicationType
Journal Article