| pubmed-article:14718571 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:14718571 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
| pubmed-article:14718571 | lifeskim:mentions | umls-concept:C0256073 | lld:lifeskim |
| pubmed-article:14718571 | lifeskim:mentions | umls-concept:C0022680 | lld:lifeskim |
| pubmed-article:14718571 | lifeskim:mentions | umls-concept:C0751283 | lld:lifeskim |
| pubmed-article:14718571 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:14718571 | pubmed:dateCreated | 2004-3-4 | lld:pubmed |
| pubmed-article:14718571 | pubmed:abstractText | Autosomal dominant polycystic kidney disease (ADPKD) is typified by the accumulation of fluid-filled cysts and abnormalities in renal epithelial cell function. The disease is principally caused by mutations in the gene encoding polycystin-1, a large basolateral plasma membrane protein expressed in kidney epithelial cells. Our studies reveal that, in normal kidney cells, polycystin-1 forms a complex with the adherens junction protein E-cadherin and its associated catenins, suggesting a role in cell adhesion or polarity. In primary cells from ADPKD patients, the polycystin-1/polycystin-2/E-cadherin/beta-catenin complex was disrupted and both polycystin-1 and E-cadherin were depleted from the plasma membrane as a result of the increased phosphorylation of polycystin-1. The loss of E-cadherin was compensated by the transcriptional upregulation of the normally mesenchymal N-cadherin. Increased cell surface N-cadherin in the disease cells in turn stabilized the continued plasma membrane localization of beta-catenin in the absence of E-cadherin. The results suggest that enhanced phosphorylation of polycystin-1 in ADPKD cells precipitates changes in its localization and its ability to form protein complexes that are critical for the stabilization of adherens junctions and the maintenance of a fully differentiated polarized renal epithelium. | lld:pubmed |
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| pubmed-article:14718571 | pubmed:language | eng | lld:pubmed |
| pubmed-article:14718571 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14718571 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:14718571 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:14718571 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:14718571 | pubmed:issn | 1059-1524 | lld:pubmed |
| pubmed-article:14718571 | pubmed:author | pubmed-author:WardChristoph... | lld:pubmed |
| pubmed-article:14718571 | pubmed:author | pubmed-author:HarrisPeter... | lld:pubmed |
| pubmed-article:14718571 | pubmed:author | pubmed-author:BacallaoRober... | lld:pubmed |
| pubmed-article:14718571 | pubmed:author | pubmed-author:Wandinger-Nes... | lld:pubmed |
| pubmed-article:14718571 | pubmed:author | pubmed-author:RoitbakTamara... | lld:pubmed |
| pubmed-article:14718571 | pubmed:author | pubmed-author:NessScott ASA | lld:pubmed |
| pubmed-article:14718571 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:14718571 | pubmed:volume | 15 | lld:pubmed |
| pubmed-article:14718571 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:14718571 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:14718571 | pubmed:pagination | 1334-46 | lld:pubmed |
| pubmed-article:14718571 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:14718571 | pubmed:meshHeading | pubmed-meshheading:14718571... | lld:pubmed |
| pubmed-article:14718571 | pubmed:meshHeading | pubmed-meshheading:14718571... | lld:pubmed |
| pubmed-article:14718571 | pubmed:meshHeading | pubmed-meshheading:14718571... | lld:pubmed |
