IndraLab
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"Western blot studies showed that the expression and activation of mTOR were both inhibited by GL-V9 ( xref E), because mTOR specifically phosphorylates the p70S6 kinase at Thr-389, the phosphorylation of p70S6 kinase at this position is a routine and specific assay for monitoring mTOR activity [ xref ]."
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"Then, mTOR phosphorylates downstream p70S6K1 Thr389 and 4E‐BP1 Thr37/46 to activate the eukaryotic initiation cytokines eIF4B and eIF4E and promote protein synthesis and muscle growth. xref Additionally, there is evidence indicating that neurotrophin 3 impacts protein synthesis and metabolic reorganization in neurogenic muscle by activating the TrkC/AKT/mTORC1 pathway in muscle fibres, as opposed to myoblasts. xref "
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"PHD3 knockdown also increased the phosphorylation of JNK at Thr 183 and Tyr 185 under basal and TNF-α-stimulated conditions (Fig. xref ) but reduced mTOR complex 1-dependent phosphorylation of p70 S6 kinase at Thr 389 , Thr 421 , and Ser 424 (ref. xref ) under insulin stimulation (Supplementary Fig. xref ), consistent with impaired insulin signalling."
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"Western blot studies showed that the expression and activation of mTOR were both inhibited by GL-V9 (XREF_FIG E), because mTOR specifically phosphorylates the p70S6 kinase at Thr 389, the phosphorylation of p70S6 kinase at this position is a routine and specific assay for monitoring mTOR activity [XREF_BIBR]."
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"Further downstream, mTOR phosphorylates p70 S6 kinase (T389), a regulator of Ribosomal Protein S6 (RPS6) responsible for mRNA translation, and has been proposed to signal via 14-3-3 (tyrosine 3-monooxygenase), a required protein in Raf signaling, to inhibit IRS-1 in a negative feedback loop XREF_BIBR."
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"[47] Following growth factor stimulation, S6K1 is phosphorylated by mTOR kinase at Thr229 on the activation loop and subsequently at Thr389 on the hydrophobic region by PDK1 [63]; once activated, S6K1 catalyzes the phosphorylation of the S6 ribosomal protein, thus playing a key role in the regulation of protein synthesis and cell growth."
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"The site at Thr389 is essential to the function of S6K1, and activated mTOR can phosphorylate S6K1 at the Thr389 residue, causing phosphorylation and recruitment of the 40S ribosomal unit and finally enhancing the translation of mRNAs, including elongation factors and ribosomal proteins XREF_BIBR."
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"In this context, activation of mTORC1 leads to increased translation and cell growth by two mechanisms : first, phosphorylation of Thr 389 of S6K1 by mTOR results in activation of S6K1 and subsequent phosphorylation of five evolutionarily conserved residues (Ser235, Ser236, Ser240, Ser244, and Ser247) of ribosomal protein S6 (RPS6) that activates RPS6."