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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
7
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pubmed:dateCreated |
1999-10-21
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pubmed:abstractText |
Crk-associated substrate (Cas) lymphocyte-type (Cas-L) is a 105-kDa cytoplasmic protein consisting of Src homology-3 domain and multiple YXXP motifs (substrate domain). Our previous studies showed that Cas-L is tyrosine-phosphorylated following the ligation of TCR and beta 1 integrins in T lymphocytes. Here we show that Cas-L is involved in T cell motility following the ligation of TCR and beta 1 integrin. Peripheral T lymphocytes showed a marked increase of migration on fibronectin (FN) after the ligation of TCR. In contrast, the migrating Jurkat cells, in which Cas-L was marginally expressed, were less than one-tenth in number on the same condition. Transfection of wild-type Cas-L into Jurkat cells resulted in restoring CD3 plus FN-induced cell migration. Furthermore, following the ligation of beta 1 integrin alone, the Cas-L transfectants significantly migrated better than the vector control. Mutational analysis of Cas-L revealed that the substrate domain is required for both FN- and CD3-induced tyrosine phosphorylation of Cas-L and cell migration caused by FN alone and CD3 plus FN. In contrast, the Src homology-3 domain is required only for the FN-induced tyrosine phosphorylation of Cas-L and cell migration, but not for CD3-induced tyrosine phosphorylation or CD3 plus FN-induced cell migration. These data strongly suggest that Cas-L is a key molecule in T cell migration induced by the ligation of CD3 and beta 1 integrins and that tyrosine phosphorylation of Cas-L is essential for T cell migration.
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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 |
AIM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Signal Transducing,
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD29,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD3,
http://linkedlifedata.com/resource/pubmed/chemical/Fibronectins,
http://linkedlifedata.com/resource/pubmed/chemical/Integrin alpha4beta1,
http://linkedlifedata.com/resource/pubmed/chemical/Integrin alpha5,
http://linkedlifedata.com/resource/pubmed/chemical/Integrins,
http://linkedlifedata.com/resource/pubmed/chemical/NEDD9 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-myc,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Antigen, T-Cell,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Fibronectin,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Lymphocyte Homing,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0022-1767
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
163
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3727-34
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:10490968-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:10490968-Antibodies, Monoclonal,
pubmed-meshheading:10490968-Antigens, CD,
pubmed-meshheading:10490968-Antigens, CD29,
pubmed-meshheading:10490968-Antigens, CD3,
pubmed-meshheading:10490968-Cell Migration Inhibition,
pubmed-meshheading:10490968-Cell Movement,
pubmed-meshheading:10490968-Fibronectins,
pubmed-meshheading:10490968-Humans,
pubmed-meshheading:10490968-Integrin alpha4beta1,
pubmed-meshheading:10490968-Integrin alpha5,
pubmed-meshheading:10490968-Integrins,
pubmed-meshheading:10490968-Jurkat Cells,
pubmed-meshheading:10490968-Phosphoproteins,
pubmed-meshheading:10490968-Phosphorylation,
pubmed-meshheading:10490968-Proto-Oncogene Proteins c-myc,
pubmed-meshheading:10490968-Receptors, Antigen, T-Cell,
pubmed-meshheading:10490968-Receptors, Fibronectin,
pubmed-meshheading:10490968-Receptors, Lymphocyte Homing,
pubmed-meshheading:10490968-T-Lymphocytes,
pubmed-meshheading:10490968-Transfection,
pubmed-meshheading:10490968-Tyrosine
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pubmed:year |
1999
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pubmed:articleTitle |
Tyrosine phosphorylation of Crk-associated substrate lymphocyte-type is a critical element in TCR- and beta 1 integrin-induced T lymphocyte migration.
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pubmed:affiliation |
Division of Tumor Immunology, Dana-Farber Cancer Institute, Department of Medicine, Harvard Medical School, Boston, MA 02115, 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
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