Gene interactions and pathways from curated databases and text-mining
Science 1997, PMID: 9204908

Phosphorylation of the translational repressor PHAS-I by the mammalian target of rapamycin.

Brunn, G J; Hudson, C C; Sekulić, A; Williams, J M; Hosoi, H; Houghton, P J; Lawrence, J C; Abraham, R T

The immunosuppressant rapamycin interferes with G1-phase progression in lymphoid and other cell types by inhibiting the function of the mammalian target of rapamycin (mTOR). mTOR was determined to be a terminal kinase in a signaling pathway that couples mitogenic stimulation to the phosphorylation of the eukaryotic initiation factor (eIF)-4E-binding protein, PHAS-I. The rapamycin-sensitive protein kinase activity of mTOR was required for phosphorylation of PHAS-I in insulin-stimulated human embryonic kidney cells. mTOR phosphorylated PHAS-I on serine and threonine residues in vitro, and these modifications inhibited the binding of PHAS-I to eIF-4E. These studies define a role for mTOR in translational control and offer further insights into the mechanism whereby rapamycin inhibits G1-phase progression in mammalian cells.

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Text Mining Data

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Manually curated Databases

  • NCI Pathway Database mTOR signaling pathway: mTORC1 complex (MTOR-MLST8-RPTOR) → 4E-BP1/eIF4E complex (EIF4EBP1-EIF4E) (modification, activates)
    Evidence: mutant phenotype, assay, physical interaction
In total, 10 gene pairs are associated to this article in curated databases