| pubmed-article:20808760 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:20808760 | lifeskim:mentions | umls-concept:C0521009 | lld:lifeskim |
| pubmed-article:20808760 | lifeskim:mentions | umls-concept:C0379710 | lld:lifeskim |
| pubmed-article:20808760 | lifeskim:mentions | umls-concept:C0010853 | lld:lifeskim |
| pubmed-article:20808760 | lifeskim:mentions | umls-concept:C1511695 | lld:lifeskim |
| pubmed-article:20808760 | lifeskim:mentions | umls-concept:C0243144 | lld:lifeskim |
| pubmed-article:20808760 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
| pubmed-article:20808760 | lifeskim:mentions | umls-concept:C1533157 | lld:lifeskim |
| pubmed-article:20808760 | pubmed:issue | 8 | lld:pubmed |
| pubmed-article:20808760 | pubmed:dateCreated | 2010-9-2 | lld:pubmed |
| pubmed-article:20808760 | pubmed:abstractText | 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. | lld:pubmed |
| pubmed-article:20808760 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20808760 | pubmed:language | eng | lld:pubmed |
| pubmed-article:20808760 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20808760 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:20808760 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20808760 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20808760 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20808760 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20808760 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20808760 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20808760 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:20808760 | pubmed:issn | 1545-7885 | lld:pubmed |
| pubmed-article:20808760 | pubmed:author | pubmed-author:ThornHansH | lld:pubmed |
| pubmed-article:20808760 | pubmed:author | pubmed-author:BrinkmannVolk... | lld:pubmed |
| pubmed-article:20808760 | pubmed:author | pubmed-author:MeyerThomas... | lld:pubmed |
| pubmed-article:20808760 | pubmed:author | pubmed-author:ChurinYuriY | lld:pubmed |
| pubmed-article:20808760 | pubmed:author | pubmed-author:KirchnerMarie... | lld:pubmed |
| pubmed-article:20808760 | pubmed:author | pubmed-author:BoettcherJan... | lld:pubmed |
| pubmed-article:20808760 | pubmed:author | pubmed-author:KaushanskyAle... | lld:pubmed |
| pubmed-article:20808760 | pubmed:author | pubmed-author:MacbeathGavin... | lld:pubmed |
| pubmed-article:20808760 | pubmed:author | pubmed-author:PompaiahMalvi... | lld:pubmed |
| pubmed-article:20808760 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:20808760 | pubmed:volume | 8 | lld:pubmed |
| pubmed-article:20808760 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:20808760 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:20808760 | pubmed:meshHeading | pubmed-meshheading:20808760... | lld:pubmed |
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| pubmed-article:20808760 | pubmed:meshHeading | pubmed-meshheading:20808760... | lld:pubmed |
| pubmed-article:20808760 | pubmed:meshHeading | pubmed-meshheading:20808760... | lld:pubmed |
| pubmed-article:20808760 | pubmed:meshHeading | pubmed-meshheading:20808760... | lld:pubmed |
| pubmed-article:20808760 | pubmed:meshHeading | pubmed-meshheading:20808760... | lld:pubmed |
| pubmed-article:20808760 | pubmed:meshHeading | pubmed-meshheading:20808760... | lld:pubmed |
| pubmed-article:20808760 | pubmed:meshHeading | pubmed-meshheading:20808760... | lld:pubmed |
| pubmed-article:20808760 | pubmed:meshHeading | pubmed-meshheading:20808760... | lld:pubmed |
| pubmed-article:20808760 | pubmed:meshHeading | pubmed-meshheading:20808760... | lld:pubmed |
| pubmed-article:20808760 | pubmed:year | 2010 | lld:pubmed |
| pubmed-article:20808760 | pubmed:articleTitle | Tyrosine-phosphorylated caveolin-1 blocks bacterial uptake by inducing Vav2-RhoA-mediated cytoskeletal rearrangements. | lld:pubmed |
| pubmed-article:20808760 | pubmed:affiliation | Department of Molecular Biology, Max Planck Institute for Infection Biology, Berlin, Germany. | lld:pubmed |
| pubmed-article:20808760 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:20808760 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:20808760 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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