| pubmed-article:11408571 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11408571 | lifeskim:mentions | umls-concept:C0205145 | lld:lifeskim |
| pubmed-article:11408571 | lifeskim:mentions | umls-concept:C1154382 | lld:lifeskim |
| pubmed-article:11408571 | lifeskim:mentions | umls-concept:C0271510 | lld:lifeskim |
| pubmed-article:11408571 | lifeskim:mentions | umls-concept:C0667316 | lld:lifeskim |
| pubmed-article:11408571 | lifeskim:mentions | umls-concept:C1420744 | lld:lifeskim |
| pubmed-article:11408571 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:11408571 | pubmed:dateCreated | 2001-6-15 | lld:pubmed |
| pubmed-article:11408571 | pubmed:abstractText | ZO-1 is an actin filament (F-actin)-binding protein that localizes to tight junctions and connects claudin to the actin cytoskeleton in epithelial cells. In nonepithelial cells that have no tight junctions, ZO-1 localizes to adherens junctions (AJs) and may connect cadherin to the actin cytoskeleton indirectly through beta- and alpha-catenins as one of many F-actin-binding proteins. Nectin is an immunoglobulin-like adhesion molecule that localizes to AJs and is associated with the actin cytoskeleton through afadin, an F-actin-binding protein. Ponsin is an afadin- and vinculin-binding protein that also localizes to AJs. The nectin-afadin complex has a potency to recruit the E-cadherin-beta-catenin complex through alpha-catenin in a manner independent of ponsin. By the use of cadherin-deficient L cell lines stably expressing various components of the cadherin-catenin and nectin-afadin systems, and alpha-catenin-deficient F9 cell lines, we examined here whether nectin recruits ZO-1 to nectin-based cell-cell adhesion sites. Nectin showed a potency to recruit not only alpha-catenin but also ZO-1 to nectin-based cell-cell adhesion sites. This recruitment of ZO-1 was dependent on afadin but independent of alpha-catenin and ponsin. These results indicate that ZO-1 localizes to cadherin-based AJs through interactions not only with alpha-catenin but also with the nectin-afadin system. | lld:pubmed |
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| pubmed-article:11408571 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11408571 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11408571 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11408571 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11408571 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11408571 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:11408571 | pubmed:issn | 1059-1524 | lld:pubmed |
| pubmed-article:11408571 | pubmed:author | pubmed-author:YamamotoYY | lld:pubmed |
| pubmed-article:11408571 | pubmed:author | pubmed-author:TakaiYY | lld:pubmed |
| pubmed-article:11408571 | pubmed:author | pubmed-author:NakanishiHH | lld:pubmed |
| pubmed-article:11408571 | pubmed:author | pubmed-author:YokoyamaSS | lld:pubmed |
| pubmed-article:11408571 | pubmed:author | pubmed-author:IrieKK | lld:pubmed |
| pubmed-article:11408571 | pubmed:author | pubmed-author:TachibanaKK | lld:pubmed |
| pubmed-article:11408571 | pubmed:author | pubmed-author:MondenMM | lld:pubmed |
| pubmed-article:11408571 | pubmed:author | pubmed-author:MandaiKK | lld:pubmed |
| pubmed-article:11408571 | pubmed:author | pubmed-author:NagafuchiAA | lld:pubmed |
| pubmed-article:11408571 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11408571 | pubmed:volume | 12 | lld:pubmed |
