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rdf:type |
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lifeskim:mentions |
umls-concept:C0024501,
umls-concept:C0105770,
umls-concept:C0178539,
umls-concept:C0300423,
umls-concept:C0721534,
umls-concept:C1167622,
umls-concept:C1292733,
umls-concept:C1332729,
umls-concept:C1442792,
umls-concept:C1513143,
umls-concept:C1519726
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pubmed:issue |
36
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pubmed:dateCreated |
2005-9-13
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pubmed:abstractText |
In several pathological conditions, epithelial cells demonstrate a breakdown of barrier function and acquire an invasive phenotype. Endothelial cells in particular are maintained in a mesenchymal state during the cell invasion phase of angiogenesis. We show here that tyrosine phosphorylation of the adherens junction protein VE-cadherin at two critical tyrosines, Tyr-658 and Tyr-731, via tyrosine kinase activation or phosphatase inactivation was sufficient to prevent the binding of p120- and beta-catenin, respectively, to the cytoplasmic tail of VE-cadherin. In fact, phosphorylation at either site led to the inhibition of cell barrier function. Cells expressing wild-type VE-cadherin showed decreased cell migration compared with cells lacking VE-cadherin, whereas expression of VE-cadherin with a simple phosphomimetic tyrosine-to-glutamic acid mutation of Y658E or Y731E was sufficient to restore the migratory response. These findings demonstrate that a single phosphorylation event within the VE-cadherin cytoplasmic tail is sufficient to maintain cells in a mesenchymal state.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD,
http://linkedlifedata.com/resource/pubmed/chemical/CTNNB1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Cadherins,
http://linkedlifedata.com/resource/pubmed/chemical/Catenins,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Adhesion Molecules,
http://linkedlifedata.com/resource/pubmed/chemical/Cytoskeletal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine,
http://linkedlifedata.com/resource/pubmed/chemical/beta Catenin,
http://linkedlifedata.com/resource/pubmed/chemical/cadherin 5,
http://linkedlifedata.com/resource/pubmed/chemical/delta catenin,
http://linkedlifedata.com/resource/pubmed/chemical/src-Family Kinases
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
9
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pubmed:volume |
280
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
31906-12
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:16027153-Amino Acid Sequence,
pubmed-meshheading:16027153-Animals,
pubmed-meshheading:16027153-Antigens, CD,
pubmed-meshheading:16027153-CHO Cells,
pubmed-meshheading:16027153-Cadherins,
pubmed-meshheading:16027153-Catenins,
pubmed-meshheading:16027153-Cell Adhesion Molecules,
pubmed-meshheading:16027153-Cell Movement,
pubmed-meshheading:16027153-Cricetinae,
pubmed-meshheading:16027153-Cytoplasm,
pubmed-meshheading:16027153-Cytoskeletal Proteins,
pubmed-meshheading:16027153-Genes, Reporter,
pubmed-meshheading:16027153-Humans,
pubmed-meshheading:16027153-Molecular Sequence Data,
pubmed-meshheading:16027153-Mutation,
pubmed-meshheading:16027153-Phosphoproteins,
pubmed-meshheading:16027153-Phosphorylation,
pubmed-meshheading:16027153-Protein Binding,
pubmed-meshheading:16027153-Protein Structure, Tertiary,
pubmed-meshheading:16027153-Trans-Activators,
pubmed-meshheading:16027153-Tyrosine,
pubmed-meshheading:16027153-beta Catenin,
pubmed-meshheading:16027153-src-Family Kinases
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pubmed:year |
2005
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pubmed:articleTitle |
Tyrosine phosphorylation of VE-cadherin prevents binding of p120- and beta-catenin and maintains the cellular mesenchymal state.
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pubmed:affiliation |
Moores Cancer Center, University of California at San Diego, La Jolla, California 92093, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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