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MTOR phosphorylates RPS6KB1. 10 / 508
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"Some studies suggest that mTOR can directly phosphorylate its effectors, such as S6K1 and 4E-BP1, while others claim that the mTOR dependent phosphorylation of S6K1 and 4E-BP1 is an indirect result of the inhibition of PP2A [XREF_BIBR; XREF_BIBR]."

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"Phosphorylation of S6K1 by mTOR in the heart is mediated by the mTOR complex 1 (mTORC1), which is sensitive to rapamycin."

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"42 However, inhibition of mTOR by some chemicals, such as rapa, will promote AKT phosphorylation by blocking the phosphorylation of insulin receptor substrate 1 and p70 ribosoma S6 kinase, XREF_BIBR, XREF_BIBR which are known to be a part of a negative feedback mechanism of PI3K-AKT signal transduction."

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"In mTORC1, mTOR binds to Raptor, mLST8 and PRAS40, and phosphorylates the translational factors S6K-1 and 4E-BP1 [XREF_BIBR], regulating different cell processes in response to nutrients and/or growth factors [XREF_BIBR]."

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"As previously reported in cancer cells (Mamane et al., 2006), Mtor could induce phosphorylation of p70S6K, Eif4ebp1 and cause their dissociation from Eif3 and Eif4e respectively, inducing the translat[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"When mTOR phosphorylates p70S6K, this kinase phosphorylates S6 ribosomal protein in return [XREF_BIBR, 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 ."

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"An inhibitor of the mammalian target of rapamycin (mTOR) blocked the stretch induced phosphorylation of p70S6K but did not affect the eEF2 activation."

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"To activate the translational cascade, mTOR phosphorylates S6 kinase (S6K1), which is liberated from the eIF3-complex and mobilized for activation of its downstream targets."

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"Interestingly, the study has also found that autophagy activators decrease the cytotoxicity of fenofibrate, while autophagy inhibitors increase the fenofibrate-induced glioblastoma cytotoxicity including phosphorylation of AMPK and suppression of mTOR- dependent phosphorylation of p70S6K ( xref )."