| pubmed-article:12927518 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12927518 | lifeskim:mentions | umls-concept:C0036953 | lld:lifeskim |
| pubmed-article:12927518 | lifeskim:mentions | umls-concept:C0105770 | lld:lifeskim |
| pubmed-article:12927518 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:12927518 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:12927518 | lifeskim:mentions | umls-concept:C1145667 | lld:lifeskim |
| pubmed-article:12927518 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:12927518 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:12927518 | lifeskim:mentions | umls-concept:C1707271 | lld:lifeskim |
| pubmed-article:12927518 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:12927518 | pubmed:dateCreated | 2003-8-20 | lld:pubmed |
| pubmed-article:12927518 | pubmed:abstractText | IpaC of Shigella is essential for initial bacterial entry into epithelial cells. We report here that IpaC interacts with beta-catenin and destabilizes the cadherin-mediated cell adhesion complex. Using a yeast two-hybrid system, we identified beta-catenin as a binding partner of IpaC within the host cell after cell entry, but not in the initial entry. Co-immunoprecipitation, confocal microscopy, and GST pull-down experiments confirmed the intracellular and cell-free interactions between these two proteins. The interaction sites were mapped to the ninth armadillo repeat of beta-catenin and to the C-terminus of IpaC. IpaC-associated beta-catenin was phosphorylated at tyrosine residues. This phosphorylation led to the destabilization of the functional cadherin-catenin complex, which could be a mechanism whereby the epithelial cell-cell tight adhesion is disrupted. These events may facilitate the further basolateral invasion of bacteria through the disrupted space and/or modulate the cell-to-cell spread of Shigella. | lld:pubmed |
| pubmed-article:12927518 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12927518 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12927518 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12927518 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12927518 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12927518 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12927518 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12927518 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12927518 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12927518 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12927518 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12927518 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:12927518 | pubmed:issn | 0882-4010 | lld:pubmed |
| pubmed-article:12927518 | pubmed:author | pubmed-author:WatanabeHaruo... | lld:pubmed |
| pubmed-article:12927518 | pubmed:author | pubmed-author:TerajimaJunJ | lld:pubmed |
| pubmed-article:12927518 | pubmed:author | pubmed-author:ShaikhNurmoha... | lld:pubmed |
| pubmed-article:12927518 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12927518 | pubmed:volume | 35 | lld:pubmed |
| pubmed-article:12927518 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12927518 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12927518 | pubmed:pagination | 107-17 | lld:pubmed |
| pubmed-article:12927518 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:12927518 | pubmed:meshHeading | pubmed-meshheading:12927518... | lld:pubmed |
| pubmed-article:12927518 | pubmed:meshHeading | pubmed-meshheading:12927518... | lld:pubmed |
| pubmed-article:12927518 | pubmed:meshHeading | pubmed-meshheading:12927518... | lld:pubmed |
| pubmed-article:12927518 | pubmed:meshHeading | pubmed-meshheading:12927518... | lld:pubmed |
| pubmed-article:12927518 | pubmed:meshHeading | pubmed-meshheading:12927518... | lld:pubmed |
| pubmed-article:12927518 | pubmed:meshHeading | pubmed-meshheading:12927518... | lld:pubmed |
| pubmed-article:12927518 | pubmed:meshHeading | pubmed-meshheading:12927518... | lld:pubmed |
| pubmed-article:12927518 | pubmed:meshHeading | pubmed-meshheading:12927518... | lld:pubmed |
| pubmed-article:12927518 | pubmed:meshHeading | pubmed-meshheading:12927518... | lld:pubmed |
| pubmed-article:12927518 | pubmed:meshHeading | pubmed-meshheading:12927518... | lld:pubmed |
| pubmed-article:12927518 | pubmed:meshHeading | pubmed-meshheading:12927518... | lld:pubmed |
| pubmed-article:12927518 | pubmed:meshHeading | pubmed-meshheading:12927518... | lld:pubmed |
| pubmed-article:12927518 | pubmed:meshHeading | pubmed-meshheading:12927518... | lld:pubmed |
| pubmed-article:12927518 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:12927518 | pubmed:articleTitle | IpaC of Shigella binds to the C-terminal domain of beta-catenin. | lld:pubmed |
| pubmed-article:12927518 | pubmed:affiliation | Department of Bacteriology, National Institute of Infectious Diseases, 1-23-1 Toyama, Shinjuku-ku, Tokyo 162-8640, Japan. | lld:pubmed |
| pubmed-article:12927518 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12927518 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:1499 | entrezgene:pubmed | pubmed-article:12927518 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:12927518 | lld:entrezgene |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:12927518 | lld:pubmed |
