Linked Life Data

17140407

Source:http://linkedlifedata.com/resource/pubmed/id/17140407

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2007-2-22
pubmed:abstractText
The signalling pathway for the hepatocyte growth factor receptor, Met/HGF-R, is hijacked by the bacterial surface protein InlB to induce Listeria monocytogenes entry into non-phagocytic cells. We previously showed that Listeria invades host cells by interacting with specialized microdomains of the host plasma membrane called lipid rafts. In this study, we analysed in living cells signalling events that are crucial for Listeria entry using a fluorescence resonance energy transfer-based microscopic method. Phosphoinositide (PI) 3-kinase activity and Rac1 signalling induced by Listeria interacting with epithelial cells were monitored as well as signalling induced by soluble InlB and the Met natural ligand HGF. We found that InlB and HGF induced similar kinetics of PI 3-kinase and Rac1 activation. PI 3-kinase activation was upstream and independent of Rac1 activation. Cholesterol-depletion experiments were performed to address the role of lipid rafts in Met signalling. The amount of 3'-phosphoinositides produced by PI 3-kinase was not affected by cholesterol depletion, while their membrane dynamic was cholesterol-dependent. Rac1 activation, downstream from PI 3-kinase, was cholesterol-dependent suggesting that the spatial distribution of 3'-phosphoinositides within membrane microdomains is critical for Rac1 activation and consequently for F-actin assembly at bacterial entry site.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1462-5814
pubmed:author
pubmed:issnType
Print
pubmed:volume
9
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
790-803
pubmed:dateRevised
2011-8-1
pubmed:meshHeading
pubmed-meshheading:17140407-Animals, pubmed-meshheading:17140407-Bacterial Proteins, pubmed-meshheading:17140407-Cercopithecus aethiops, pubmed-meshheading:17140407-Cholesterol, pubmed-meshheading:17140407-Fluorescence Resonance Energy Transfer, pubmed-meshheading:17140407-Kinetics, pubmed-meshheading:17140407-Listeria monocytogenes, pubmed-meshheading:17140407-Luminescent Proteins, pubmed-meshheading:17140407-Membrane Microdomains, pubmed-meshheading:17140407-Membrane Proteins, pubmed-meshheading:17140407-Microscopy, Fluorescence, pubmed-meshheading:17140407-Phosphatidylinositol 3-Kinases, pubmed-meshheading:17140407-Proto-Oncogene Proteins c-met, pubmed-meshheading:17140407-Signal Transduction, pubmed-meshheading:17140407-Transfection, pubmed-meshheading:17140407-Vero Cells, pubmed-meshheading:17140407-rac1 GTP-Binding Protein
pubmed:year
2007
pubmed:articleTitle
A FRET analysis to unravel the role of cholesterol in Rac1 and PI 3-kinase activation in the InlB/Met signalling pathway.
pubmed:affiliation
Institute Pasteur, Unité des Interactions Bactéries-Cellules, Paris, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural