Source:http://linkedlifedata.com/resource/pubmed/id/16777847
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
33
|
| pubmed:dateCreated |
2006-8-14
|
| 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.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Aug
|
| pubmed:issn |
0021-9258
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
18
|
| pubmed:volume |
281
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
23824-9
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:16777847-ADAM Proteins,
pubmed-meshheading:16777847-Adherens Junctions,
pubmed-meshheading:16777847-Amino Acid Sequence,
pubmed-meshheading:16777847-Amyloid Precursor Protein Secretases,
pubmed-meshheading:16777847-Animals,
pubmed-meshheading:16777847-Basement Membrane,
pubmed-meshheading:16777847-Cattle,
pubmed-meshheading:16777847-Cell Adhesion,
pubmed-meshheading:16777847-Cell Communication,
pubmed-meshheading:16777847-Cell Line,
pubmed-meshheading:16777847-Cell Movement,
pubmed-meshheading:16777847-Dogs,
pubmed-meshheading:16777847-Endopeptidases,
pubmed-meshheading:16777847-Intracellular Fluid,
pubmed-meshheading:16777847-Molecular Sequence Data,
pubmed-meshheading:16777847-Mutagenesis, Site-Directed,
pubmed-meshheading:16777847-Protein Sorting Signals,
pubmed-meshheading:16777847-Protein Structure, Tertiary,
pubmed-meshheading:16777847-Signal Transduction,
pubmed-meshheading:16777847-Wound Healing
|
| pubmed:year |
2006
|
| pubmed:articleTitle |
A basolateral sorting signal directs ADAM10 to adherens junctions and is required for its function in cell migration.
|
| 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.
|
| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|