"It is unknown whether C. elegans LIN-3 and EGF signaling activates PI3K (AAP-1, PDK-1, and AGE-1 in C. elegans) or Akt (AKT-1 and AKT-2 in C. elegans); however, Insulin and IGF Signaling (IIS) has been implicated in regulating longevity through PI3K and Akt [XREF_BIBR]."

"However, while LY294002 inhibited Akt-1 activation by EGF, neither FTI nor RhoB-GG were effectual in blocking this activity (see Fig. 4A )."

"For example, EGF simulation induces activation of protein kinase B (PKB and Akt) via PIPs, which have multiple functions including antiapoptotic properties."

"EGF activates AKT1 ( xref ) and PTN11, the protein tyrosine phosphatase non-receptor type 11 also known as PTP2C ( xref )."

"Because ligand stimulated IGF-IR cells are not motile, we examined the effects of Akt1 or -2 overexpression on parental MCF-10A cells treated with EGF, which induces robust migration and strong activation of ERK."

"Our conclusion is supported by the following lines of evidence: (1) FBXW2 binds to β-catenin under physiological conditions, and FBXW2-β-catenin binding is dependent on an evolutionarily conserved FBXW2 consensus binding motif (TSMGGT) on β-catenin (Fig.  xref ); (2) FBXW2 ectopic expression or siRNA knockdown decreases or increases the levels of total and phosphorylated β-catenin (β-catenin pS552 ), and β-catenin transcriptional activity, respectively (Fig.  xref ); (3) FBXW2 ectopic expression or siRNA knockdown shortens or extends the protein half-lives of both β-catenin and β-catenin pS552 , respectively, and FBXW2 promotes β-catenin polyubiquitylation via K48 linkage for degradation (Fig.  xref ); (4) EGF-activated AKT1 is responsible for β-catenin phosphorylation on Ser552, which facilitates its FBXW2 binding for degradation."

"Expression of wild-type (wt) Cbp remarkably suppressed EGF-induced activation of Src, ERK1/2, and Akt-1 enzymes, and NIH3T3 cell transformation, as well as colony formation of a breast cancer cell line (MDA-MB-468) in soft agar."

"In heat-shocked cells, PKBalpha was activated to a certain level without phosphorylation on Thr-308 in the activation loop and on Thr-450 and Ser-473 in the carboxyl-terminal end region, which is critical for growth-factor-induced activation of PKBalpha."

"In summary, these studies indicate that EGF signaling through EGFR activates PKBalpha and AKT as a principal target, and blocking this pathway with the EGFR specific tyrosine kinase inhibitor, Iressa, results in programmed cell death."

"There is growing evidence that epidermal growth factor (EGF) activates Akt and protein kinase B (PKB) in a phosphoinositide 3-OH kinase (PI3K)-dependent manner, but it is not yet clear which Akt isoforms are involved in this signal transduction pathway."

"Modified assertion"

"Figure 4 shows the inhibitory effect of gefitinib on EGFinduced autophosphorylation of EGFR, and phophorylation of Akt and ERK1/2 in three of the NSCLC cell lines. EGF stimulated EGFR autophosphorylation and activation of Akt and ERK1/2 in PC9 (A), A549 (B), and QG56 (C) cells, and activation was blocked to different extents by gefitinib."

"Western blotting with the anti-phospho-Akt1 antibody, which recognizes only phosphorylated Ser-473 residue, was performed in human esophageal cancer cell lines (TE-2, TE-5, TE-8, TE-9, TE-10, and TE-12 cells) (top panel). PDGF-treated NIH3T3 cells served as a positive control. The phospho-Akt antibody demonstrated two bands at 60 kDa. The phosphorylation of Akt was enhanced by EGF stimulation in all the esophageal cancer cell lines examined, although TE-5 cells showed high basal phosphorylation of Akt."