| pubmed-article:16777847 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16777847 | lifeskim:mentions | umls-concept:C0887872 | lld:lifeskim |
| pubmed-article:16777847 | lifeskim:mentions | umls-concept:C1622501 | lld:lifeskim |
| pubmed-article:16777847 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:16777847 | lifeskim:mentions | umls-concept:C1412181 | lld:lifeskim |
| pubmed-article:16777847 | lifeskim:mentions | umls-concept:C1522688 | lld:lifeskim |
| pubmed-article:16777847 | lifeskim:mentions | umls-concept:C0439851 | lld:lifeskim |
| pubmed-article:16777847 | lifeskim:mentions | umls-concept:C1552596 | lld:lifeskim |
| pubmed-article:16777847 | lifeskim:mentions | umls-concept:C1546857 | lld:lifeskim |
| pubmed-article:16777847 | lifeskim:mentions | umls-concept:C1947931 | lld:lifeskim |
| pubmed-article:16777847 | lifeskim:mentions | umls-concept:C1556066 | lld:lifeskim |
| pubmed-article:16777847 | lifeskim:mentions | umls-concept:C1619636 | lld:lifeskim |
| pubmed-article:16777847 | lifeskim:mentions | umls-concept:C1514873 | lld:lifeskim |
| pubmed-article:16777847 | pubmed:issue | 33 | lld:pubmed |
| pubmed-article:16777847 | pubmed:dateCreated | 2006-8-14 | lld:pubmed |
| pubmed-article:16777847 | pubmed:abstractText | ADAM10 (a disintegrin and metalloprotease) initiates regulated intramembrane proteolysis by shedding the ectodomain of a number of different substrates. Shedding is followed by subsequent intramembrane proteolysis leading to the liberation of intracellular domains capable of nuclear signaling. ADAM10 substrates have been found at cell-cell contacts and are apparently involved in cell-cell interaction and cell migration. Here we have investigated the cellular mechanism that guides ADAM10 to substrates at cell-cell contacts. We demonstrate that intracellular trafficking of ADAM10 critically requires a novel sorting signal within its cytoplasmic domain. Sequential deletion of the cytoplasmic domain and site-directed mutagenesis suggest that a potential Src homology 3-binding domain is essential for ADAM10 sorting. In a polarized epithelial cell line this motif not only targets ADAM10 to adherens junctions but is also strictly required for ADAM10 function in E-cadherin processing and cell migration. | lld:pubmed |
| pubmed-article:16777847 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16777847 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16777847 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16777847 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16777847 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16777847 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16777847 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16777847 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16777847 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:16777847 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:16777847 | pubmed:author | pubmed-author:CapellAnjaA | lld:pubmed |
| pubmed-article:16777847 | pubmed:author | pubmed-author:HaassChristia... | lld:pubmed |
| pubmed-article:16777847 | pubmed:author | pubmed-author:Wild-BodeChri... | lld:pubmed |
| pubmed-article:16777847 | pubmed:author | pubmed-author:FellererKatri... | lld:pubmed |
| pubmed-article:16777847 | pubmed:author | pubmed-author:KuglerJohanna... | lld:pubmed |
| pubmed-article:16777847 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16777847 | pubmed:day | 18 | lld:pubmed |
| pubmed-article:16777847 | pubmed:volume | 281 | lld:pubmed |
| pubmed-article:16777847 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16777847 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16777847 | pubmed:pagination | 23824-9 | lld:pubmed |
| pubmed-article:16777847 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:16777847 | pubmed:meshHeading | pubmed-meshheading:16777847... | lld:pubmed |
| pubmed-article:16777847 | pubmed:meshHeading | pubmed-meshheading:16777847... | lld:pubmed |
| pubmed-article:16777847 | pubmed:meshHeading | pubmed-meshheading:16777847... | lld:pubmed |
| pubmed-article:16777847 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16777847 | pubmed:articleTitle | A basolateral sorting signal directs ADAM10 to adherens junctions and is required for its function in cell migration. | lld:pubmed |
| pubmed-article:16777847 | pubmed:affiliation | Adolf Butenandt Institute, Department of Biochemistry, Laboratory for Alzheimer's and Parkinson's Disease Research, Ludwig Maximilians University, Schillerstrasse 44, 80336 Munich, Germany. | lld:pubmed |
| pubmed-article:16777847 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16777847 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:282132 | entrezgene:pubmed | pubmed-article:16777847 | lld:entrezgene |
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