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EGF phosphorylates RPS6. 34 / 34
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"Furthermore, IGF-1, EGF and serum induced phosphorylation of Akt and rpS6 were also blocked by LY294002, indicating that rpS6 phosphorylation is under the regulation of PI3K-Akt signalling pathway in HEK293T cells."
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"However, EGF fails to stimulate DNA synthesis and is unable to stimulate the phosphorylation of S6 ribosomal protein in cells expressing this receptor mutant."
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"The stimulation by EGF of in situ S6 phosphorylation was also prevented by genistein."
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"Treatment of cultured astrocytes with FTI-277 significantly inhibited the EGF dependent increase in S6 kinase phosphorylation (XREF_FIG), suggesting that Rheb participates in mTORC1 activation."
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"Both EGF and angiotensin II stimulated S6 kinase activity and S6 phosphorylation."
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"Subsaturating concentrations of EGF and insulin act synergistically to stimulate both S6 phosphorylation and DNA synthesis, but qualitatively the two synergistic interactions are expressed differently."
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"Differential regulation of S6 phosphorylation by insulin and epidermal growth factor in Swiss mouse 3T3 cells : insulin activation of type 1 phosphatase."
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"IGF-1, EGF and serum stimulated the phosphorylation of Akt and rpS6, while DRAM1 dramatically inhibited the phosphorylation of Akt at Thr 308 and Ser 473 and rpS6 at Ser 235/236 and Ser 240/244."
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"Knockdown of G i2 α reduced Akt(S473) phosphorylation but did not impair phosphorylation of ERK1/2 and S6(S235/236) by EGF (Additional file xref : Figure S2)."
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"BI-D1870 showed no important change in EGF-induced phosphorylation of rpS6 and p70S6K ( Fig. 7 F and G)."
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"Insulin and epidermal growth factor (EGF) induce distinct kinetics of S6 kinase activation and S6 phosphorylation in Swiss 3T3 cells."
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"Importantly, TBKBP1 knockdown severely impaired EGF stimulated phosphorylation of mTORC1 target proteins, S6K and S6, without affecting the phosphorylation of AKT, and the mTORC1 signaling defect could be rescued by reconstituting the Tbkbp1-knockdown cells with TBKBP1 (XREF_FIG)."
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"Protease activated kinase II as the mediator of epidermal growth factor stimulated phosphorylation of ribosomal protein S6."
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"Strikingly, EGF and FGF2 activated phosphorylation of both ERK1/2 and S6 ( xref )."
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"EGF, in contrast, did not appear to activate protein kinase C, but promoted the phosphorylation of S6 and activation of the S6 kinase in both normal and protein kinase C deficient cells."
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"Oliver A. R., Ballou L. M. and Thomas G. (1988) Differential regulation of S6 phosphorylation by insulin and epidermal growth factor in Swiss mouse 3T3 cells : insulin activation of type 1 phosphatase[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"We evidenced that metformin selectively blocked the phosphorylation of S6 ribosomal protein, a downstream target of the mTOR-p70S6 kinase signalling pathway, induced by EGF without altering EGF induce[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"BI-D1870 and SL0101 showed no important change in EGF-induced phosphorylation of rpS6 and p70S6K ( Fig. 7 F and G)."
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"20 As shown in XREF_FIG to XREF_FIG, Western blot results revealed that boehmenan concentration-dependently inhibited EGF induced 70S6 and S6 phosphorylation, but did not affect the Akt phosphorylation."
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"EGF treatment could also markedly induce phosphorylation of AKT, ERK and S6, but no additive effect from cholesterol supplementation could be noted (XREF_FIG B)."
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"IGF-1, EGF and serum stimulated the phosphorylation of Akt and rpS6, while DRAM1 dramatically inhibited the phosphorylation of Akt at Thr 308 and Ser 473 and rpS6 at Ser 235/236 and Ser 240/244 (Fig.  xref d)."
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"The observation that the phosphorylation of tyrosyl residues on cellular proteins is also increased following infection provoked the suggestion that the secreted vaccinia virus growth factor bound to [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"As expected, EGF-induced phosphorylation of AKT, S6K, and S6 was abolished by Gαi1 and Gαi3 double knockouts ( Figure 1c and d )."
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"Epidermal growth factor stimulates phosphorylation of ribosomal protein S6 in serum starved Swiss 3T3 cells, leading to the formation of highly phosphorylated derivatives containing 4-5 phosphates."
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"The loss of late phase kinase activity results in decreased EGF-induced S6 phosphorylation, protein synthesis, and cell growth."
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"ThecomparablechangescausedonDNA synthesis, proteinsynthesisand S6 phosphorylation by eitherserum, EGF or PGF2, are not producedby insulin.indeed, theresultswithinsulinaloneargue that neitheractivation[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"EGF, PGF2 alpha and insulin induce the phosphorylation of identical S6 peptides in swiss mouse 3T3 cells : effect of cAMP on early sites of phosphorylation."
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"Treatment of cultured astrocytes with FTI-277 significantly inhibited the EGF-dependent increase in S6 kinase phosphorylation ( xref ), suggesting that Rheb participates in mTORC1 activation."
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"In contrast, the stimulation of RPS6 phosphorylation by EGF was partially independent of PI-3-kinase-and mTOR pathways."
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"Supplementary Fig. S9 Effect of RSK inhibitors on the EGF-induced phosphorylation of rpS6 in the presence of 20 μM U0126. (A) Serum-starved LN-18 cells were pretreated with 20 μM of the MEK inhibitor,[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"The same was the case between EGF-stimulated Akt and rpS6 phosphorylation."
| PMC
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"We determined that EGF activates phosphorylation of Akt, mTOR, p70S6 kinase, ribosomal protein S6, eIF4E and 4E-BP1 in a PI-3-kinase dependent manner, and PI-3-kinase activation may prevent lactogenic differentiation in HC11 mammary epithelial cells by regulating the synthesis of proteins."
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"Saturating concentrations of epidermal growth factor (EGF), insulin and serum each stimulate phosphorylation of the S6 ribosomal protein to the same maximal level; this is not so for DNA synthesis."
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"Biochemical analyses confirmed that CC214-1 successfully inhibited mTORC1 dependent 4E-BP1 and S6 phosphorylation in EGFRvIII-expressing GBM cells ( xref and xref , xref ), as well as blocked EGF-induced 4E-BP1 and S6 phosphorylation in GBM cells overexpressing wild type EGFR ( xref )."
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