rdf:type |
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lifeskim:mentions |
|
pubmed:issue |
14
|
pubmed:dateCreated |
2010-6-25
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pubmed:abstractText |
We studied the function of lipid rafts in generation and signaling of T-cell receptor microclusters (TCR-MCs) and central supramolecular activation clusters (cSMACs) at immunological synapse (IS). It has been suggested that lipid raft accumulation creates a platform for recruitment of signaling molecules upon T-cell activation. However, several lipid raft probes did not accumulate at TCR-MCs or cSMACs even with costimulation and the fluorescence resonance energy transfer (FRET) between TCR or LAT and lipid raft probes was not induced at TCR-MCs under the condition of positive induction of FRET between CD3 zeta and ZAP-70. The analysis of LAT mutants revealed that raft association is essential for the membrane localization but dispensable for TCR-MC formation. Careful analysis of the accumulation of raft probes in the cell interface revealed that their accumulation occurred after cSMAC formation, probably due to membrane ruffling and/or endocytosis. These results suggest that lipid rafts control protein translocation to the membrane but are not involved in the clustering of raft-associated molecules and therefore that the lipid rafts do not serve as a platform for T-cell activation.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/20498282-10398592,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20498282-10525547,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20498282-10723795,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20498282-10958781,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20498282-11395491,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20498282-11413487,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/20498282-12065839,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/20498282-12218094,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/20498282-14617356,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/20498282-15696158,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/20498282-16216891,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/20498282-9924026
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Signal Transducing,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD3,
http://linkedlifedata.com/resource/pubmed/chemical/CD3 antigen, zeta chain,
http://linkedlifedata.com/resource/pubmed/chemical/Green Fluorescent Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Lat protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Mutant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Antigen, T-Cell,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Sh2d2a protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/ZAP-70 Protein-Tyrosine Kinase,
http://linkedlifedata.com/resource/pubmed/chemical/Zap70 protein, mouse
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
1098-5549
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pubmed:author |
|
pubmed:issnType |
Electronic
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pubmed:volume |
30
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3421-9
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pubmed:dateRevised |
2011-7-19
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pubmed:meshHeading |
pubmed-meshheading:20498282-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:20498282-Animals,
pubmed-meshheading:20498282-Antigens, CD3,
pubmed-meshheading:20498282-Endocytosis,
pubmed-meshheading:20498282-Fluorescence Resonance Energy Transfer,
pubmed-meshheading:20498282-Green Fluorescent Proteins,
pubmed-meshheading:20498282-Lymphocyte Activation,
pubmed-meshheading:20498282-Macromolecular Substances,
pubmed-meshheading:20498282-Membrane Microdomains,
pubmed-meshheading:20498282-Membrane Proteins,
pubmed-meshheading:20498282-Mice,
pubmed-meshheading:20498282-Mice, Transgenic,
pubmed-meshheading:20498282-Mutant Proteins,
pubmed-meshheading:20498282-Mutation,
pubmed-meshheading:20498282-Phosphoproteins,
pubmed-meshheading:20498282-Protein Transport,
pubmed-meshheading:20498282-Receptors, Antigen, T-Cell,
pubmed-meshheading:20498282-Recombinant Fusion Proteins,
pubmed-meshheading:20498282-Signal Transduction,
pubmed-meshheading:20498282-T-Lymphocytes,
pubmed-meshheading:20498282-ZAP-70 Protein-Tyrosine Kinase
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pubmed:year |
2010
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pubmed:articleTitle |
T-cell receptor microclusters critical for T-cell activation are formed independently of lipid raft clustering.
|