Source:http://linkedlifedata.com/resource/pubmed/id/12837751
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
37
|
| pubmed:dateCreated |
2003-9-8
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| pubmed:abstractText |
alpha 4 integrins mediate increased cell migration and decreased cell spreading because the alpha 4 cytoplasmic domain (tail) binds tightly to paxillin, a signaling adaptor protein. Paxillin binding to the alpha 4 tail is blocked by alpha 4 phosphorylation at Ser988. To establish the biological role of alpha 4 phosphorylation, we reconstituted alpha 4-deficient Jurkat T cells with phosphorylation-mimicking (alpha 4(S988D)) or non-phosphorylatable (alpha 4(S988A)) mutants. alpha 4(S988D) disrupted paxillin binding and also inhibited cell migration and promoted cell spreading. In contrast, the non-phosphorylatable alpha 4(S988A) resulted in a further reduction in cell spreading; however, this mutation led to an unexpected suppression of cell migration. The suppression of cell migration by alpha 4(S988A) was ascribable to enhanced alpha 4-paxillin association, because enforced association by an alpha 4-paxillin fusion led to a phenotype similar to that of the non-phosphorylatable alpha 4(S988A) mutant. These data establish that optimal alpha 4-mediated cell migration requires both phosphorylation and dephosphorylation of the alpha 4 cytoplasmic domain to regulate the reversible binding of paxillin.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cell Adhesion Molecules,
http://linkedlifedata.com/resource/pubmed/chemical/Cytoskeletal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Integrin alpha4beta1,
http://linkedlifedata.com/resource/pubmed/chemical/PXN protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Paxillin,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphotyrosine,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
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| pubmed:status |
MEDLINE
|
| pubmed:month |
Sep
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| pubmed:issn |
0021-9258
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
12
|
| pubmed:volume |
278
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| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
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| pubmed:pagination |
34845-53
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| pubmed:dateRevised |
2006-11-15
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| pubmed:meshHeading |
pubmed-meshheading:12837751-Amino Acid Substitution,
pubmed-meshheading:12837751-Animals,
pubmed-meshheading:12837751-Binding Sites,
pubmed-meshheading:12837751-CHO Cells,
pubmed-meshheading:12837751-Cell Adhesion Molecules,
pubmed-meshheading:12837751-Cell Membrane,
pubmed-meshheading:12837751-Cricetinae,
pubmed-meshheading:12837751-Cytoskeletal Proteins,
pubmed-meshheading:12837751-Humans,
pubmed-meshheading:12837751-Integrin alpha4beta1,
pubmed-meshheading:12837751-Jurkat Cells,
pubmed-meshheading:12837751-Mutagenesis, Site-Directed,
pubmed-meshheading:12837751-Paxillin,
pubmed-meshheading:12837751-Phosphoproteins,
pubmed-meshheading:12837751-Phosphorylation,
pubmed-meshheading:12837751-Phosphotyrosine,
pubmed-meshheading:12837751-Protein Binding,
pubmed-meshheading:12837751-Recombinant Proteins,
pubmed-meshheading:12837751-T-Lymphocytes,
pubmed-meshheading:12837751-Transfection
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| pubmed:year |
2003
|
| pubmed:articleTitle |
Integrin alpha 4 beta 1-dependent T cell migration requires both phosphorylation and dephosphorylation of the alpha 4 cytoplasmic domain to regulate the reversible binding of paxillin.
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| pubmed:affiliation |
Department of Cell Biology, Division of Vascular Biology, The Scripps Research Institute, La Jolla, California 92037, 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
|