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• W1966978996 endingPage "436" @default.
• W1966978996 startingPage "429" @default.
• W1966978996 abstract "The mammalian-target-of-rapamycin (mTOR) is a multidomain protein that is important in regulating several components of the translational machinery. mTOR signalling is stimulated by hormones (e.g., insulin) and by amino acids. Our recent data suggest that TOR signalling responds to intracellular amino acids rather than to external amino acid levels. The translational repressor eukaryotic initiation factor 4E-binding protein 1 (4E-BP1) is regulated through mTOR and undergoes phosphorylation at multiple sites, which affects its function. It contains two regulatory motifs: the C-terminal TOS motif interacts with the mTOR-binding partner, raptor, and mediates phosphorylation of specific sites in 4E-BP1. However, the N-terminal RAIP motif affects a larger range of mTOR-regulated sites. Since this motif does not bind raptor, mTOR must signal to 4E-BP1 via additional mechanisms that are independent of raptor. The kinase that phosphorylates and inhibits elongation factor 2 (eEF2 kinase) is inactivated by insulin via mTOR. Insulin decreases the ability of eEF2 kinase to bind calmodulin, its essential activator, and this effect requires mTOR signalling and a novel phosphorylation site in eEF2 kinase, Ser78. Ser78 is not phosphorylated by known components of the mTOR pathway implying the existence of novel mTOR-regulated kinases that control eEF2 kinase." @default.
• W1966978996 created "2016-06-24" @default.
• W1966978996 creator A5030513468 @default.
• W1966978996 date "2004-01-01" @default.
• W1966978996 modified "2023-09-27" @default.
• W1966978996 title "mTOR-mediated regulation of translation factors by amino acids" @default.
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• W1966978996 doi "https://doi.org/10.1016/j.bbrc.2003.07.015" @default.
• W1966978996 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/14684180" @default.
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