pubmed-article:9700171 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:9700171 | lifeskim:mentions | umls-concept:C0014597 | lld:lifeskim |
pubmed-article:9700171 | lifeskim:mentions | umls-concept:C0205111 | lld:lifeskim |
pubmed-article:9700171 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
pubmed-article:9700171 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
pubmed-article:9700171 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
pubmed-article:9700171 | lifeskim:mentions | umls-concept:C0205144 | lld:lifeskim |
pubmed-article:9700171 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:9700171 | pubmed:dateCreated | 1998-9-4 | lld:pubmed |
pubmed-article:9700171 | pubmed:abstractText | alphaE-catenin, a cadherin-associated protein, is required for tight junction (TJ) organization, but its role is poorly understood. We transfected an alphaE-catenin-deficient colon carcinoma line with a series of alphaE-catenin mutant constructs. The results showed that the amino acid 326-509 domain of this catenin was required to organize TJs, and its COOH-terminal domain was not essential for this process. The 326-509 internal domain was found to bind vinculin. When an NH2-terminal alphaE-catenin fragment, which is by itself unable to organize the TJ, was fused with the vinculin tail, this chimeric molecule could induce TJ assembly in the alphaE-catenin-deficient cells. In vinculin-null F9 cells, their apical junctional organization was impaired, and this phenotype was rescued by reexpression of vinculin. These results indicate that the alphaE-catenin-vinculin interaction plays a role in the assembly of the apical junctional complex in epithelia. | lld:pubmed |
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pubmed-article:9700171 | pubmed:language | eng | lld:pubmed |
pubmed-article:9700171 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9700171 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:9700171 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9700171 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9700171 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:9700171 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:9700171 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:9700171 | pubmed:month | Aug | lld:pubmed |
pubmed-article:9700171 | pubmed:issn | 0021-9525 | lld:pubmed |
pubmed-article:9700171 | pubmed:author | pubmed-author:UemuraTT | lld:pubmed |
pubmed-article:9700171 | pubmed:author | pubmed-author:FujimotoKK | lld:pubmed |
pubmed-article:9700171 | pubmed:author | pubmed-author:van RoyFF | lld:pubmed |
pubmed-article:9700171 | pubmed:author | pubmed-author:AdamsonE DED | lld:pubmed |