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SRC phosphorylates AKT on tyrosine. 28 / 28
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"We began to test this hypothesis by assessing tyrosine phosphorylation of Akt by Src in HT1080 cells."
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"The G i/o -protein dependent PI3K activation leads to the membrane recruitment of Akt, which is phosphorylated at tyrosine (Y) by cSrc with the subsequent phosphorylation by PDK1 and mTORC2."
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"Then Src phosphorylates Akt at Y residue(s), which triggers Akt A-loop (T308) and HM (S473) phosphorylation by PDK1 and mTORC2 xref ."
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"The starting point is the Gi/o-protein dependent PI3K activation that leads to the membrane recruitment of Akt, which becomes tyrosine phosphorylated by c-Src with the subsequent phosphorylation in both the activation loop within the kinase domain [A-loop (T308)] and the hydrophobic motif in the C-terminal region [HM (S473)] by PDK1 and mTORC2, respectively."
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"Tyrosine phosphorylation of Akt by Src enhances the activity of Akt."
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"Our results support a working model in which the adaptor protein APPL1 inhibits cell migration and adhesion dynamics through a mechanism involving the Src-mediated tyrosine phosphorylation of Akt."
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"In this study, therefore, we determined quercetin inhibition on LPS-induced Src and Syk mediated PI3K tyrosine phosphorylations and Akt activation."
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"Thus, these results suggest APPL1 reduces the amount of active Akt in cells by inhibiting tyrosine phosphorylation of Akt by Src."
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"In addition, YAP1 is serine phosphorylated by AKT and JNK and tyrosine phosphorylated by Yes and Src and Abl (Basu et al., 2003; Danovi et al., 2008; Levy et al., 2008; Piccolo et al., 2014; Zhao et a[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Akt tyrosine phosphorylation is mediated by the non receptor tyrosine kinase Src."
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"Upon EGF stimulation, Akt is phosphorylated at Tyr315 and Tyr326 by Src or protein tyrosine kinase 6 (PTK6), a Src related tyrosine kinase [XREF_BIBR, XREF_BIBR]."
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"APPL1 regulates the tyrosine phosphorylation of Akt by Src."
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"In addition, APPL1 significantly decreases the tyrosine phosphorylation of Akt by the nonreceptor tyrosine kinase Src, which is critical for Akt mediated cell migration."
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"Moreover, APPL1 inhibits the ability of Akt to promote migration by impairing Src mediated tyrosine phosphorylation of Akt."
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"APPL1 regulates the tyrosine phosphorylation of Akt by Src."
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"Because tyrosine phosphorylation of Akt by Src was recently shown to be important in both the activation of Akt and its biological function, we hypothesized that Src mediated tyrosine phosphorylation of Akt was critical for its effects on migration."
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"The PKB Y315 residue, which is known to be phosphorylated by Src tyrosine kinase, was also a major site of phosphorylation by RET and PTC."
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"Thus, these results suggest APPL1 reduces the amount of active Akt in cells by inhibiting tyrosine phosphorylation of Akt by Src."
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"Thus, APPL1 can inhibit Akt function by reducing the tyrosine phosphorylation of Akt by Src, which hinders cell migration."
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"Tyrosine phosphorylation of Akt by Src enhances the activity of Akt."
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"The PKB Y315 residue, which is known to be phosphorylated by Src tyrosine kinase, was also a major site of phosphorylation by RET/PTC."
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"We began to test this hypothesis by assessing tyrosine phosphorylation of Akt by Src in HT1080 cells."
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"Because tyrosine phosphorylation of Akt by Src was recently shown to be important in both the activation of Akt and its biological function (Chen ; Choudhury ; Bouchard ), we hypothesized that Src-mediated tyrosine phosphorylation of Akt was critical for its effects on migration."
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"Somules incubated with herbimycin A, a Src inhibitor, before insulin exposure displayed supressed Akt phosphorylation at 2 hours (Figure 2C; Supplementary Figure 5), identifying Src as the likely kinase that phosphorylates Tyr within the PEYLA region (Figure 1A)."
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"However, more recent work indicates that Akt activity is also regulated by tyrosine phosphorylation, which is carried out by Src (Chen )."
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"Interestingly, our results in XREF_FIG indicate that OxPAPC mediated tyrosine phosphorylation of Akt (by Src and Fyn) (XREF_FIG) is S1P 1 receptor independent."
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"Thus, APPL1 can inhibit Akt function by reducing the tyrosine phosphorylation of Akt by Src, which hinders cell migration."
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"In our study, inhibition of Src with PP2 led to a decrease in the tyrosine phosphorylation of Akt, whereas promotion of Src activity, through expression of CA-Src, increased the level of tyrosine phosphorylated Akt, indicating that Src can tyrosine phosphorylate Akt."
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