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  Tyrosine-Phosphorylated Caveolin-1 Blocks Bacterial Uptake by Inducing Vav2-RhoA-Mediated Cytoskeletal Rearrangements

Boettcher, J. P., Kirchner, M., Churin, Y., Kaushansky, A., Pompaiah, M., Thorn, H., et al. (2010). Tyrosine-Phosphorylated Caveolin-1 Blocks Bacterial Uptake by Inducing Vav2-RhoA-Mediated Cytoskeletal Rearrangements. PLoS Biology, 8(8): e1000457.

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Genre: Journal Article
Alternative Title : PLoS. Biol.

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Copyright: © 2010 Boettcher et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
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 Creators:
Boettcher, Jan Peter1, Author              
Kirchner, Marieluise1, Author              
Churin, Yuri1, Author              
Kaushansky, Alexis, Author
Pompaiah, Malvika1, Author              
Thorn, Hans1, Author              
Brinkmann, Volker2, Author              
MacBeath, Gavin, Author
Meyer, Thomas F.1, Author              
Affiliations:
1Department of Molecular Biology, Max Planck Institute for Infection Biology, Max Planck Society, ou_1664147              
2Core Facilities / Microscopy, Max Planck Institute for Infection Biology, Max Planck Society, ou_1664142              

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 Abstract: Certain bacterial adhesins appear to promote a pathogen's extracellular lifestyle rather than its entry into host cells. However, little is known about the stimuli elicited upon such pathogen host-cell interactions. Here, we report that type IV pili (Tfp)-producing Neisseria gonorrhoeae (P(+)GC) induces an immediate recruitment of caveolin-1 (Cav1) in the host cell, which subsequently prevents bacterial internalization by triggering cytoskeletal rearrangements via downstream phosphotyrosine signaling. A broad and unbiased analysis of potential interaction partners for tyrosine-phosphorylated Cav1 revealed a direct interaction with the Rho-family guanine nucleotide exchange factor Vav2. Both Vav2 and its substrate, the small GTPase RhoA, were found to play a direct role in the Cav1-mediated prevention of bacterial uptake. Our findings, which have been extended to enteropathogenic Escherichia coli, highlight how Tfp-producing bacteria avoid host cell uptake. Further, our data establish a mechanistic link between Cav1 phosphorylation and pathogen-induced cytoskeleton reorganization and advance our understanding of caveolin function.

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Language(s): eng - English
 Dates: 2010-08
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 531855
ISI: 000281464500013
 Degree: -

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Title: PLoS Biology
  Alternative Title : PLoS. Biol.
Source Genre: Journal
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Pages: - Volume / Issue: 8 (8) Sequence Number: e1000457 Start / End Page: - Identifier: ISSN: 1544-9173