IndraLab

Statements

SRC phosphorylates AKT on Y315. 9 / 9
2 | 3 3 1
sparser
"We also showed that phosphorylation of Tyr-315 in Akt induced by Src or EGF is dependent on the integrity of this proline-rich motif."
12600984
signor
"We also showed that phosphorylation of Tyr-315 in Akt induced by Src or EGF is dependent on the integrity of this proline-rich motif. Furthermore, the Akt mutant lacking this proline motif fails to block the transcription activity of Forkhead in 293 cells and poorly stimulates the proliferation of Madin-Darby canine kidney cells. Taken together, our data suggest that the interaction between the SH3 domain of Src family kinases and the proline-rich motif in the C-terminal regulatory region of Akt is required for tyrosine phosphorylation of Akt and its subsequent activation."
12600984
rlimsp
"Because previous work showed that the major Src phosphorylation sites in Akt, which are important in regulating its activity and function, are tyrosines 315 and 326 (Chen ), we mutated these tyrosine residues to phenylalanines."
22379109
reach
"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]."
25309720
signor
"Regulation of Akt/PKB Activation by Tyrosine PhosphorylationAs shown in Fig. 2 d, while mutation of Tyr340 has little effect on either tyrosine phosphorylation or kinase activity of Akt induced by Src527F, substitution of Tyr315 or Tyr326 with a phenylalanine, respectively, dramatically reduces both the tyrosine phosphorylation and kinase activity of Akt. The combination of these two mutations abolishes Src-induced tyrosine phosphorylation of Akt as well as its kinase activity."
11445557
sparser
"Upon EGF stimulation, Akt is phosphorylated at Tyr315 and Tyr326 by Src or protein tyrosine kinase 6 (PTK6), a Src-related tyrosine kinase [ xref , xref ]."
25309720
reach
"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."
15994200
sparser
"The complex allows c-Src to phosphorylate Tyr315 and 326 residues of Akt, which are necessary for subsequent phosphorylation of Akt on thr308 and ser473 by PDK1 and PDK2, separately ( xref )."
35096302
reach
"We also showed that phosphorylation of Tyr 315 in Akt induced by Src or EGF is dependent on the integrity of this proline rich motif."
12600984