Document Detail


A FRET analysis to unravel the role of cholesterol in Rac1 and PI 3-kinase activation in the InlB/Met signalling pathway.
MedLine Citation:
PMID:  17140407     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
Stéphanie Seveau; To N Tham; Bernard Payrastre; Adam D Hoppe; Joel A Swanson; Pascale Cossart
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2006-11-28
Journal Detail:
Title:  Cellular microbiology     Volume:  9     ISSN:  1462-5814     ISO Abbreviation:  Cell. Microbiol.     Publication Date:  2007 Mar 
Date Detail:
Created Date:  2007-02-22     Completed Date:  2007-06-26     Revised Date:  2014-09-10    
Medline Journal Info:
Nlm Unique ID:  100883691     Medline TA:  Cell Microbiol     Country:  England    
Other Details:
Languages:  eng     Pagination:  790-803     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Animals
Bacterial Proteins / physiology*
Cercopithecus aethiops
Cholesterol / metabolism*,  physiology
Fluorescence Resonance Energy Transfer / methods*
Kinetics
Listeria monocytogenes / physiology
Luminescent Proteins / genetics,  metabolism
Membrane Microdomains / metabolism,  microbiology
Membrane Proteins / physiology*
Microscopy, Fluorescence
Phosphatidylinositol 3-Kinases / metabolism*
Proto-Oncogene Proteins c-met / physiology*
Signal Transduction*
Transfection
Vero Cells
rac1 GTP-Binding Protein / metabolism*
Grant Support
ID/Acronym/Agency:
AI35950/AI/NIAID NIH HHS; R01 AI035950/AI/NIAID NIH HHS; R01 AI035950-14/AI/NIAID NIH HHS; R01 AI064668/AI/NIAID NIH HHS; R01 AI064668-03/AI/NIAID NIH HHS
Chemical
Reg. No./Substance:
0/Bacterial Proteins; 0/Luminescent Proteins; 0/Membrane Proteins; 0/inlB protein, Listeria monocytogenes; 97C5T2UQ7J/Cholesterol; EC 2.7.1.-/Phosphatidylinositol 3-Kinases; EC 2.7.10.1/Proto-Oncogene Proteins c-met; EC 3.6.5.2/rac1 GTP-Binding Protein

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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