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rdf:type |
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lifeskim:mentions |
umls-concept:C0039194,
umls-concept:C0332281,
umls-concept:C0439680,
umls-concept:C0542341,
umls-concept:C0871161,
umls-concept:C1425360,
umls-concept:C1514873,
umls-concept:C1546857,
umls-concept:C1556066,
umls-concept:C1619636,
umls-concept:C1879547
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pubmed:issue |
1
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pubmed:dateCreated |
2002-6-21
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pubmed:abstractText |
2B4 is a receptor belonging to the Ig superfamily and is found on all murine NK cells as well as a small subset of T cells. Previous studies have found that cross-linking of the 2B4 receptor results in both increased cytotoxicity and IFN-gamma secretion. We have discovered that 2B4 from transfected NK and T cell lines, as well as from primary murine cells, coimmunoprecipitates with the phosphoprotein linker for the activation of T cells (LAT), which is essential for TCR-mediated signaling. This association is independent of both 2B4 phosphorylation and the cytoplasmic tail of 2B4. We have found that, along with LAT, 2B4 is constitutively located in glycolipid-enriched microdomains of the plasma membrane. In fact, 2B4 appears to associate with LAT only when it localizes to glycolipid-enriched microdomains. This localization of 2B4 occurs due to a CxC cysteine motif found in the transmembrane region, as determined by mutagenesis studies. 2B4-mediated cytotoxicity is defective in the absence of LAT, indicating that LAT is a required intermediate for 2B4 signal transduction. However, we have also shown that LAT association alone is not sufficient for maximal 2B4 activation.
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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/Antigens, CD,
http://linkedlifedata.com/resource/pubmed/chemical/CD244 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cd244 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Glycolipids,
http://linkedlifedata.com/resource/pubmed/chemical/LAT protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Lat protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Isoforms,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Immunologic
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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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 |
169
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
55-62
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:12077228-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:12077228-Animals,
pubmed-meshheading:12077228-Antigens, CD,
pubmed-meshheading:12077228-Carrier Proteins,
pubmed-meshheading:12077228-Cell Line,
pubmed-meshheading:12077228-Cytoplasm,
pubmed-meshheading:12077228-Cytotoxicity, Immunologic,
pubmed-meshheading:12077228-Glycolipids,
pubmed-meshheading:12077228-Humans,
pubmed-meshheading:12077228-Jurkat Cells,
pubmed-meshheading:12077228-Killer Cells, Natural,
pubmed-meshheading:12077228-Lymphocyte Activation,
pubmed-meshheading:12077228-Membrane Glycoproteins,
pubmed-meshheading:12077228-Membrane Microdomains,
pubmed-meshheading:12077228-Membrane Proteins,
pubmed-meshheading:12077228-Mice,
pubmed-meshheading:12077228-Mice, Inbred C57BL,
pubmed-meshheading:12077228-Mice, Knockout,
pubmed-meshheading:12077228-Mice, SCID,
pubmed-meshheading:12077228-Mutagenesis, Site-Directed,
pubmed-meshheading:12077228-Phosphoproteins,
pubmed-meshheading:12077228-Phosphorylation,
pubmed-meshheading:12077228-Protein Isoforms,
pubmed-meshheading:12077228-Protein Structure, Tertiary,
pubmed-meshheading:12077228-Receptors, Immunologic,
pubmed-meshheading:12077228-T-Lymphocytes,
pubmed-meshheading:12077228-Transfection
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pubmed:year |
2002
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pubmed:articleTitle |
2B4 is constitutively associated with linker for the activation of T cells in glycolipid-enriched microdomains: properties required for 2B4 lytic function.
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pubmed:affiliation |
Department of Pathology and Graduate Program in Immunology, University of Texas Southwestern Medical Center, Dallas, TX 75390-9072, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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