pubmed-article:16339173 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:16339173 | lifeskim:mentions | umls-concept:C0044602 | lld:lifeskim |
pubmed-article:16339173 | lifeskim:mentions | umls-concept:C0887872 | lld:lifeskim |
pubmed-article:16339173 | lifeskim:mentions | umls-concept:C0282639 | lld:lifeskim |
pubmed-article:16339173 | lifeskim:mentions | umls-concept:C2936824 | lld:lifeskim |
pubmed-article:16339173 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
pubmed-article:16339173 | lifeskim:mentions | umls-concept:C0033414 | lld:lifeskim |
pubmed-article:16339173 | lifeskim:mentions | umls-concept:C1710082 | lld:lifeskim |
pubmed-article:16339173 | lifeskim:mentions | umls-concept:C1879748 | lld:lifeskim |
pubmed-article:16339173 | lifeskim:mentions | umls-concept:C1706853 | lld:lifeskim |
pubmed-article:16339173 | pubmed:issue | Pt 1 | lld:pubmed |
pubmed-article:16339173 | pubmed:dateCreated | 2005-12-22 | lld:pubmed |
pubmed-article:16339173 | pubmed:abstractText | Human intestinal cell differentiation is mediated by signaling pathways that remain largely undefined. We and others have shown that cell migration and differentiation along the crypt-villus axis is associated with temporal and spatial modulations of the repertoire, as well as with the function of integrins and E-cadherins and their substrates. Cross-talk between integrin and cadherin signaling was previously described and seems to coordinate this differentiation process. Here, we report that engagement of alpha6 and, to a lesser extent, alpha3 integrin subunits after HT-29 cell adhesion on laminin 5 increases the expression of E-cadherin, which then organizes into nascent adherens junctions. We further identify that phosphoinositide 3-kinase (PI 3-kinase) activation plays a key role in this cross-talk. Indeed, integrin-dependent adhesion on laminin 5 stimulates PI 3-kinase activity. Immunofluorescence and immunoprecipitation experiments revealed that activated PI 3-kinase is recruited at cell-cell contacts. Using LY294002, an inhibitor of PI 3-kinase activity, we found that this activation is essential for E-cadherin connection with the cytoskeleton and for biogenesis of adherens junctions. Finally, we demonstrated that PI 3-kinase could signal through Rac1b activation to control adherens junction assembly. Our results provide a mechanistic insight into integrin-cadherin cross-talk and identify a novel role for PI 3-kinase in the establishment of adherens junctions. | lld:pubmed |
pubmed-article:16339173 | pubmed:language | eng | lld:pubmed |
pubmed-article:16339173 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16339173 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:16339173 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16339173 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16339173 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16339173 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:16339173 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:16339173 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:16339173 | pubmed:month | Jan | lld:pubmed |
pubmed-article:16339173 | pubmed:issn | 0021-9533 | lld:pubmed |
pubmed-article:16339173 | pubmed:author | pubmed-author:BlockMarc RMR | lld:pubmed |
pubmed-article:16339173 | pubmed:author | pubmed-author:MatosPauloP | lld:pubmed |
pubmed-article:16339173 | pubmed:author | pubmed-author:ChartierNicol... | lld:pubmed |
pubmed-article:16339173 | pubmed:author | pubmed-author:LainéMichèleM | lld:pubmed |
pubmed-article:16339173 | pubmed:author | pubmed-author:GoutStéphanie... | lld:pubmed |
pubmed-article:16339173 | pubmed:author | pubmed-author:PawlakGéraldi... | lld:pubmed |
pubmed-article:16339173 | pubmed:author | pubmed-author:MarieChristia... | lld:pubmed |
pubmed-article:16339173 | pubmed:author | pubmed-author:Jacquier-Sarl... | lld:pubmed |
pubmed-article:16339173 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:16339173 | pubmed:day | 1 | lld:pubmed |
pubmed-article:16339173 | pubmed:volume | 119 | lld:pubmed |
pubmed-article:16339173 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:16339173 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:16339173 | pubmed:pagination | 31-46 | lld:pubmed |
pubmed-article:16339173 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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pubmed-article:16339173 | pubmed:year | 2006 | lld:pubmed |
pubmed-article:16339173 | pubmed:articleTitle | Laminin-5-integrin interaction signals through PI 3-kinase and Rac1b to promote assembly of adherens junctions in HT-29 cells. | lld:pubmed |
pubmed-article:16339173 | pubmed:affiliation | Laboratoire d'Etude de la Différenciation et de l'Adhérence Cellulaires, UMR UJF/CNRS 5538, Institut Albert Bonniot, Faculté de Médecine de Grenoble, Domaine de la Merci, 38706 La Tronche Cedex, France. | lld:pubmed |
pubmed-article:16339173 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:16339173 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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