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All rights reserved. http://resource.belframework.org/belframework/1.0/knowledge/large_corpus.bel http://purl.org/dc/elements/1.1/title BEL Framework Large Corpus Document http://resource.belframework.org/belframework/1.0/knowledge/large_corpus.bel http://purl.org/pav/authoredBy http://www.tkuhn.ch/bel2nanopub/RAyj4F1OPIF_NCCxdgBV6Hr37mKH2NMa509c4HxvOgmcY#_5 http://resource.belframework.org/belframework/1.0/knowledge/large_corpus.bel http://purl.org/pav/version 1.4 http://www.tkuhn.ch/bel2nanopub/RAyj4F1OPIF_NCCxdgBV6Hr37mKH2NMa509c4HxvOgmcY#_4 http://www.w3.org/ns/prov#value exogenously provided PA stimulated the activation of the mTORsubs trate S6 kinase and phosphorylation of another mTORsubs trate eukaryotic initiation factor 4E binding protein-1 (4E-BP1) in HEK293 cells. The effect of PA was sensitive to rapamycin (3, 8) and was dependent on the presence of amino acids (3). The amino acid dependence indicated that the effect of PA was physiologic. Subsequently, Blenis group similarly showed that PA stimulated S6 kinase activity in HEK293 cells (9). The ability of PA to stimulate S6 kinase was suppressed by coexpression of TSC1/2, also suggesting that the PA-induced S6 kinase activity was physiologic. 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