| pubmed-article:10525547 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10525547 | lifeskim:mentions | umls-concept:C1167250 | lld:lifeskim |
| pubmed-article:10525547 | lifeskim:mentions | umls-concept:C0034790 | lld:lifeskim |
| pubmed-article:10525547 | lifeskim:mentions | umls-concept:C0037083 | lld:lifeskim |
| pubmed-article:10525547 | lifeskim:mentions | umls-concept:C1710082 | lld:lifeskim |
| pubmed-article:10525547 | lifeskim:mentions | umls-concept:C0332621 | lld:lifeskim |
| pubmed-article:10525547 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:10525547 | pubmed:dateCreated | 1999-11-17 | lld:pubmed |
| pubmed-article:10525547 | pubmed:abstractText | The role of lipid rafts in T cell antigen receptor (TCR) signaling was investigated using fluorescence microscopy. Lipid rafts labeled with cholera toxin B subunit (CT-B) and cross-linked into patches displayed characteristics of rafts isolated biochemically, including detergent resistance and colocalization with raft-associated proteins. LCK, LAT, and the TCR all colocalized with lipid patches, although TCR association was sensitive to nonionic detergent. Aggregation of the TCR by anti-CD3 mAb cross-linking also caused coaggregation of raft-associated proteins. However, the protein tyrosine phosphatase CD45 did not colocalize to either CT-B or CD3 patches. Cross-linking of either CD3 or CT-B strongly induced tyrosine phosphorylation and recruitment of a ZAP-70(SH2)(2)-green fluorescent protein (GFP) fusion protein to the lipid patches. Also, CT-B patching induced signaling events analagous to TCR stimulation, with the same dependence on expression of key TCR signaling molecules. Targeting of LCK to rafts was necessary for these events, as a nonraft- associated transmembrane LCK chimera, which did not colocalize with TCR patches, could not reconstitute CT-B-induced signaling. Thus, our results indicate a mechanism whereby TCR engagement promotes aggregation of lipid rafts, which facilitates colocalization of LCK, LAT, and the TCR whilst excluding CD45, thereby triggering protein tyrosine phosphorylation. | lld:pubmed |
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| pubmed-article:10525547 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10525547 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10525547 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10525547 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10525547 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10525547 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10525547 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:10525547 | pubmed:issn | 0021-9525 | lld:pubmed |
| pubmed-article:10525547 | pubmed:author | pubmed-author:MageeA IAI | lld:pubmed |
| pubmed-article:10525547 | pubmed:author | pubmed-author:PAZM RMR | lld:pubmed |
| pubmed-article:10525547 | pubmed:author | pubmed-author:JanesP WPW | lld:pubmed |
| pubmed-article:10525547 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10525547 | pubmed:day | 18 | lld:pubmed |
| pubmed-article:10525547 | pubmed:volume | 147 | lld:pubmed |
| pubmed-article:10525547 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10525547 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10525547 | pubmed:pagination | 447-61 | lld:pubmed |
| pubmed-article:10525547 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:10525547 | pubmed:meshHeading | pubmed-meshheading:10525547... | lld:pubmed |
| pubmed-article:10525547 | pubmed:meshHeading | pubmed-meshheading:10525547... | lld:pubmed |
