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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
51
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pubmed:dateCreated |
1996-1-30
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pubmed:abstractText |
Two molecules involved in signal transduction via the T cell antigen receptor, namely the protein-tyrosine kinase ZAP-70 and the proto-oncoprotein Vav, were found to be constitutively associated with tubulin in Jurkat T cells. Both were able to bind to tubulin independently of one another, as determined by transient transfection into COS-7 cells. The ZAP-70 associated with tubulin was preferentially tyrosine-phosphorylated after T cell antigen receptor stimulation of Jurkat T cells, suggesting that this interaction was functionally significant. Vav was also found to co-immunoprecipitate with ZAP-70 from cell extracts depleted of tubulin. This raised the possibility that Vav might be a substrate for ZAP-70 protein-tyrosine kinase activity. However, tyrosine phosphorylation of Vav preceded that of ZAP-70, indicating that Vav was unlikely to be a downstream target of ZAP-70. The association of ZAP-70 and Vav with tubulin implies that the microtubules may be involved in the signaling function of these two molecules, perhaps by targeting them to their appropriate intracellular location.
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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/Cell Cycle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Immunosuppressive Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Muromonab-CD3,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphotyrosine,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-vav,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Antigen, T-Cell,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tubulin,
http://linkedlifedata.com/resource/pubmed/chemical/VAV1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/ZAP-70 Protein-Tyrosine Kinase,
http://linkedlifedata.com/resource/pubmed/chemical/ZAP70 protein, human
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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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 |
22
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pubmed:volume |
270
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
30241-4
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:8530437-Animals,
pubmed-meshheading:8530437-Cell Cycle Proteins,
pubmed-meshheading:8530437-Cell Line,
pubmed-meshheading:8530437-Cercopithecus aethiops,
pubmed-meshheading:8530437-Cloning, Molecular,
pubmed-meshheading:8530437-Cytosol,
pubmed-meshheading:8530437-Humans,
pubmed-meshheading:8530437-Immunosuppressive Agents,
pubmed-meshheading:8530437-Muromonab-CD3,
pubmed-meshheading:8530437-Phosphorylation,
pubmed-meshheading:8530437-Phosphotyrosine,
pubmed-meshheading:8530437-Protein-Tyrosine Kinases,
pubmed-meshheading:8530437-Proto-Oncogene Proteins,
pubmed-meshheading:8530437-Proto-Oncogene Proteins c-vav,
pubmed-meshheading:8530437-Receptors, Antigen, T-Cell,
pubmed-meshheading:8530437-Recombinant Proteins,
pubmed-meshheading:8530437-T-Lymphocytes,
pubmed-meshheading:8530437-Transfection,
pubmed-meshheading:8530437-Tubulin,
pubmed-meshheading:8530437-Tumor Cells, Cultured,
pubmed-meshheading:8530437-ZAP-70 Protein-Tyrosine Kinase
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pubmed:year |
1995
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pubmed:articleTitle |
Interactions between the protein-tyrosine kinase ZAP-70, the proto-oncoprotein Vav, and tubulin in Jurkat T cells.
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pubmed:affiliation |
Division of Cellular Immunology, National Institute for Medical Research, Mill Hill, London, United Kingdom.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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