Source:http://linkedlifedata.com/resource/pubmed/id/20663922
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
Pt 16
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pubmed:dateCreated |
2010-8-5
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pubmed:abstractText |
Epithelial junctions are dynamically and functionally linked to the actin cytoskeleton, and their disassembly is a key event during physiological and pathological processes. We recently showed that epithelial disintegration facilitates transcriptional activation via Rac, G-actin, MAL (also known as MRTF) and serum response factor (SRF). Here, we investigate which specific component of the epithelial junction is essential for this MAL-SRF-mediated transcription. The Ca(2+)-dependent dissociation of polarised epithelial cells depleted of ZO proteins - which form adherens junctions (AJs) but completely lack tight junctions (TJs) - fully activated SRF. By contrast, AGS gastric adenocarcinoma epithelial cells, which form TJs but are deficient in E-cadherin, and therefore also in AJs, failed to activate SRF. The introduction of wild-type E-cadherin in AGS cells restored AJ formation and MAL-SRF inducibility. To gain further insight into the membrane-proximal signalling, AGS cells were stably transfected with E-cadherin-alpha-catenin fusions. Despite restored formation of cell-cell contacts containing the nectin-afadin complex and p120-catenin, these cells did not activate SRF upon junction dissociation, suggesting that signal transmission depends on the C-terminal tail of E-cadherin. We conclude that the dissociation of intercellular E-cadherin interactions from AJs, and signals originating from the C-terminal region covering the beta-catenin-binding site of E-cadherin, are essential for transcriptional activation via Rac, MAL and SRF, whereas TJs are not involved.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cadherins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/MKL1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/MKL1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Oncogene Proteins, Fusion,
http://linkedlifedata.com/resource/pubmed/chemical/Serum Response Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators,
http://linkedlifedata.com/resource/pubmed/chemical/alpha Catenin,
http://linkedlifedata.com/resource/pubmed/chemical/beta Catenin
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
1477-9137
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:day |
15
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pubmed:volume |
123
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2803-9
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pubmed:meshHeading |
pubmed-meshheading:20663922-Adherens Junctions,
pubmed-meshheading:20663922-Animals,
pubmed-meshheading:20663922-Cadherins,
pubmed-meshheading:20663922-Cell Line,
pubmed-meshheading:20663922-DNA-Binding Proteins,
pubmed-meshheading:20663922-Epithelial Cells,
pubmed-meshheading:20663922-Gene Expression,
pubmed-meshheading:20663922-Humans,
pubmed-meshheading:20663922-Mice,
pubmed-meshheading:20663922-Oncogene Proteins, Fusion,
pubmed-meshheading:20663922-Serum Response Factor,
pubmed-meshheading:20663922-Tight Junctions,
pubmed-meshheading:20663922-Trans-Activators,
pubmed-meshheading:20663922-Transcription, Genetic,
pubmed-meshheading:20663922-Transfection,
pubmed-meshheading:20663922-alpha Catenin,
pubmed-meshheading:20663922-beta Catenin
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pubmed:year |
2010
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pubmed:articleTitle |
E-cadherin regulates MAL-SRF-mediated transcription in epithelial cells.
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pubmed:affiliation |
Department of Molecular Biology, AG Regulation of Gene Expression, Max Planck Institute of Biochemistry, D-82152 Martinsried, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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