pubmed-article:7515100 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:7515100 | lifeskim:mentions | umls-concept:C0007600 | lld:lifeskim |
pubmed-article:7515100 | lifeskim:mentions | umls-concept:C0044602 | lld:lifeskim |
pubmed-article:7515100 | lifeskim:mentions | umls-concept:C0039194 | lld:lifeskim |
pubmed-article:7515100 | lifeskim:mentions | umls-concept:C0021764 | lld:lifeskim |
pubmed-article:7515100 | lifeskim:mentions | umls-concept:C0282625 | lld:lifeskim |
pubmed-article:7515100 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
pubmed-article:7515100 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
pubmed-article:7515100 | pubmed:issue | 6 | lld:pubmed |
pubmed-article:7515100 | pubmed:dateCreated | 1994-6-27 | lld:pubmed |
pubmed-article:7515100 | pubmed:abstractText | The proliferation of antigen-activated T cells is mediated by the T cell-derived growth factor, interleukin 2 (IL-2). The biochemical signaling cascades initiating IL-2-induced growth are dependent upon protein tyrosine kinase (PTK) activity. One IL-2-regulated PTK implicated in this cascade is the Src-family kinase, Fyn. Previous studies have described a physical association between Fyn and a potential downstream substrate, phosphatidylinositol 3-kinase (PI3-kinase) as well as the IL-2-dependent activation of PI3-kinase in T cells; however, the role of Fyn in IL-2-induced PI3-kinase activation remains unclear. In this report, we demonstrate that IL-2 stimulation triggers tyrosine phosphorylation of the p85 subunit of PI3-kinase in the murine T cell line, CTLL-2. Lysates prepared from growth factor-deprived and IL-2-stimulated T cells reconstituted both the binding of CTLL-2 cell-derived Fyn to and the IL-2-inducible tyrosine phosphorylation of exogenously added recombinant p85. Furthermore, overexpression of wild-type Fyn in these cells enhanced both the basal and IL-2-mediated activation of PI3-kinase. Additional studies of the Fyn-PI3-kinase interaction demonstrated that the Src homology 3 (SH3) domain of Fyn constitutes a direct binding site for the p85 subunit of PI3-kinase. These results support the notion that Fyn may be directly involved in the activation of the downstream signaling enzyme, PI3-kinase, in IL-2-stimulated T cells. | lld:pubmed |
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pubmed-article:7515100 | pubmed:language | eng | lld:pubmed |
pubmed-article:7515100 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7515100 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:7515100 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:7515100 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7515100 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7515100 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7515100 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7515100 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7515100 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7515100 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:7515100 | pubmed:month | Jun | lld:pubmed |
pubmed-article:7515100 | pubmed:issn | 0022-1007 | lld:pubmed |
pubmed-article:7515100 | pubmed:author | pubmed-author:AbrahamR TRT | lld:pubmed |
pubmed-article:7515100 | pubmed:author | pubmed-author:KarnitzL MLM | lld:pubmed |
pubmed-article:7515100 | pubmed:author | pubmed-author:SutorS LSL | lld:pubmed |
pubmed-article:7515100 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:7515100 | pubmed:day | 1 | lld:pubmed |
pubmed-article:7515100 | pubmed:volume | 179 | lld:pubmed |
pubmed-article:7515100 | pubmed:geneSymbol | lck | lld:pubmed |
pubmed-article:7515100 | pubmed:geneSymbol | fyn | lld:pubmed |
pubmed-article:7515100 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:7515100 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:7515100 | pubmed:pagination | 1799-808 | lld:pubmed |
pubmed-article:7515100 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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