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rdf:type |
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lifeskim:mentions |
umls-concept:C0037083,
umls-concept:C0109317,
umls-concept:C0162493,
umls-concept:C0752312,
umls-concept:C1150579,
umls-concept:C1155065,
umls-concept:C1333340,
umls-concept:C1366882,
umls-concept:C1367475,
umls-concept:C1370600,
umls-concept:C1421567,
umls-concept:C1425844,
umls-concept:C1514873,
umls-concept:C1546857,
umls-concept:C1556066,
umls-concept:C1619636,
umls-concept:C1705767,
umls-concept:C1705791,
umls-concept:C1710082,
umls-concept:C1879547,
umls-concept:C1948023
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pubmed:issue |
6
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pubmed:dateCreated |
2000-10-4
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pubmed:abstractText |
Activation of T cells can be initiated through cell surface molecules in addition to the T-cell receptor-CD3 (TCR-CD3) complex. In human T cells, ligation of the CD2 molecule by mitogenic pairs of anti-CD2 monoclonal antibodies activates T cells via biochemical signaling pathways similar but not identical to those elicited on TCR engagement. This study describes a key role for the p36/38 membrane adapter protein linker for T cell activation (LAT) in CD2-mediated T-cell activation. Following ligation of CD2 on the surface of the Jurkat T-cell line and human purified T cells, LAT was tyrosine phosphorylated and shown to associate in vivo with a number of other tyrosine phosphorylated proteins including PLCgamma-1, Grb-2, and SLP-76. Using Jurkat cell lines deficient in ZAP70/Syk (P116) or LAT (ANJ3) expression, CD2-dependent PLCgamma-1 and SLP-76 tyrosine phosphorylation required expression both of ZAP70 or Syk and of LAT. As predicted, the absence of either LAT or ZAP70/Syk kinases correlated with a defect in the induction of nuclear factor of activated T cells (NFAT) transcriptional activity, activation of the interleukin-2 promoter, and ERK phosphorylation following CD2 stimulation. These data suggest that LAT is an adapter protein important for the regulation of CD2-mediated T-cell activation.
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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/Antigens, CD2,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Precursors,
http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/LAT protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/NFATC Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Syk kinase,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
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 |
Sep
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pubmed:issn |
0006-4971
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
96
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2181-90
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pubmed:dateRevised |
2011-11-2
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pubmed:meshHeading |
pubmed-meshheading:10979964-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:10979964-Antigens, CD2,
pubmed-meshheading:10979964-Carrier Proteins,
pubmed-meshheading:10979964-DNA-Binding Proteins,
pubmed-meshheading:10979964-Enzyme Precursors,
pubmed-meshheading:10979964-Humans,
pubmed-meshheading:10979964-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:10979964-Jurkat Cells,
pubmed-meshheading:10979964-Lymphocyte Activation,
pubmed-meshheading:10979964-Membrane Proteins,
pubmed-meshheading:10979964-Mitogen-Activated Protein Kinases,
pubmed-meshheading:10979964-NFATC Transcription Factors,
pubmed-meshheading:10979964-Nuclear Proteins,
pubmed-meshheading:10979964-Phosphoproteins,
pubmed-meshheading:10979964-Protein-Tyrosine Kinases,
pubmed-meshheading:10979964-Signal Transduction,
pubmed-meshheading:10979964-T-Lymphocytes,
pubmed-meshheading:10979964-Transcription Factors,
pubmed-meshheading:10979964-Transcriptional Activation,
pubmed-meshheading:10979964-ZAP-70 Protein-Tyrosine Kinase
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pubmed:year |
2000
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pubmed:articleTitle |
Signaling via LAT (linker for T-cell activation) and Syk/ZAP70 is required for ERK activation and NFAT transcriptional activation following CD2 stimulation.
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pubmed:affiliation |
Laboratory of Lymphocyte Biology, National Heart, Lung, and Blood Institute, Laboratory of Cellular and Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, MD.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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