| pubmed-article:8895571 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8895571 | lifeskim:mentions | umls-concept:C0037083 | lld:lifeskim |
| pubmed-article:8895571 | lifeskim:mentions | umls-concept:C0031621 | lld:lifeskim |
| pubmed-article:8895571 | lifeskim:mentions | umls-concept:C0021467 | lld:lifeskim |
| pubmed-article:8895571 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:8895571 | lifeskim:mentions | umls-concept:C1414805 | lld:lifeskim |
| pubmed-article:8895571 | lifeskim:mentions | umls-concept:C0439851 | lld:lifeskim |
| pubmed-article:8895571 | lifeskim:mentions | umls-concept:C1710082 | lld:lifeskim |
| pubmed-article:8895571 | lifeskim:mentions | umls-concept:C0021469 | lld:lifeskim |
| pubmed-article:8895571 | lifeskim:mentions | umls-concept:C0243077 | lld:lifeskim |
| pubmed-article:8895571 | lifeskim:mentions | umls-concept:C1552596 | lld:lifeskim |
| pubmed-article:8895571 | lifeskim:mentions | umls-concept:C1947931 | lld:lifeskim |
| pubmed-article:8895571 | lifeskim:mentions | umls-concept:C0078517 | lld:lifeskim |
| pubmed-article:8895571 | lifeskim:mentions | umls-concept:C0251991 | lld:lifeskim |
| pubmed-article:8895571 | pubmed:issue | 19 | lld:pubmed |
| pubmed-article:8895571 | pubmed:dateCreated | 1996-12-16 | lld:pubmed |
| pubmed-article:8895571 | pubmed:abstractText | The immunosuppressant, rapamycin, inhibits cell growth by interfering with the function of a novel kinase, termed mammalian target of rapamycin (mTOR). The putative catalytic domain of mTOR is similar to those of mammalian and yeast phosphatidylinositol (PI) 3-kinases. This study demonstrates that mTOR is a component of a cytokine-triggered protein kinase cascade leading to the phosphorylation of the eukaryotic initiation factor-4E (eIF-4E) binding protein, PHAS-1, in activated T lymphocytes. This event promotes G1 phase progression by stimulating eIF-4E-dependent translation initiation. A mutant YAC-1 T lymphoma cell line, which was selected for resistance to the growth-inhibitory action of rapamycin, was correspondingly resistant to the suppressive effect of this drug on PHAS-1 phosphorylation. In contrast, the PI 3-kinase inhibitor, wortmannin, reduced the phosphorylation of PHAS-1 in both rapamycin-sensitive and -resistant T cells. At similar drug concentrations (0.1-1 microM), wortmannin irreversibly inhibited the serine-specific autokinase activity of mTOR. The autokinase activity of mTOR was also sensitive to the structurally distinct PI 3-kinase inhibitor, LY294002, at concentrations (1-30 microM) nearly identical to those required for inhibition of the lipid kinase activity of the mammalian p85-p110 heterodimer. These studies indicate that the signaling functions of mTOR, and potentially those of other high molecular weight PI 3-kinase homologs, are directly affected by cellular treatment with wortmannin or LY294002. | lld:pubmed |
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| pubmed-article:8895571 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:8895571 | pubmed:citationSubset | IM | lld:pubmed |
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