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SRC phosphorylates AKT on tyrosine. 16 / 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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"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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"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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"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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"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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