IndraLab

"In a similar way, small molecule compound screens could be done to test for drugs that can specifically disrupt EGFR-Grb2 interactions upon EGF-stimulation ( xref )."

"Preclinical studies revealed cetuximab could decrease cell proliferation and phosphorylation of EGFR, and blocked the binding of the adaptor protein Grb2 to EGFR upon activation by EGF [ xref ]."

"Interestingly, in spite of the free phosphonate group with its negative charges, CGP78850 inhibited association of Grb2 with EGFR in intact serum-starved MDA-MB-468 triple-negative breast cancer cells stimulated with EGF in vitro ."

"Our results support the concept that EGFR interacts with Grb2 in both constitutive and EGF-dependent manners and this interaction is independent of HER3 co-expression."

"1) Association of Grb2 to EGFR in BxPC-3 induced by EGF in the presence of Erbitux indicates an alternate pathway of Ras-MAPK activation, which may be related with the tumor resistance to treatment; 2) transactivation of EGFR downstream Ras-MAPK pathway by FGF contributes the resistance to treatment; and 3) downregulation of EGFR may increase the response to therapy."

"Because Ras activation by EGF involves EGF-stimulated association of EGF-R with Grb2, the EGF-R was immunoprecipitated and a Western blot was probed for Grb2."

"To demonstrate the utility of rsTagRFP as a switchable pcFRET acceptor, we next studied the interaction between EGFR and Grb2 that is induced upon stimulation with epidermal growth factor (EGF) in mammalian cells."

"This aspect of the model is consistent with the conventional view that adaptors bind exposed phosphotyrosine residues on receptors and our experiments showing that there is only measurable FRET between EGFR and Grb2 after EGF stimulation."

"Upon EGF stimulation, Grb2 binds phosphorylated EGFR and activates the signaling pathway xref , xref ."

"Together these data indicate that AG-1478 inhibits both constitutive as well as EGF-induced EGFR-Grb2 interaction."

"In the present study the function of Ash/Grb-2 was investigated by microinjecting cells with an anti-Ash antibody. The antibody abolished both S phase entry and the reorganization of actin assembly to ruffle formation upon stimulation with epidermal growth factor (EGF) and platelet-derived growth factor (PDGF). On the other hand, anti-Ash antibody had no effect on S phase entry or actin stress fiber formation induced by either serum or lysophosphatidic acid. Since the induction of DNA synthesis, ruffle induction and stress fiber formation involve a function of Ras, Rac activation and Rho activation respectively, the findings strongly suggest that Ash plays a critical role in the signaling of both pathways downstream from growth factor receptors to Ras and Rac. Consistent with this, Ash co-precipitated with EGF receptor from EGF-stimulated cells."

"Compound inhibited epidermal growth factor (EGF)-induced protein–protein interactions between EGFR (EGF receptor) and Grb2 in MDA-MB-468 cells and inhibited Ras activation in the same cell line."

"We identified that As 2 O 3 activates EGFR and promotes phosphorylation of p66 ShcA and its interaction with the Grb2 adaptor protein with slower kinetics compared to EGF-mediated EGFR activation."

"Pre-clinical studies showed cetuximab decreased cell proliferation and phosphorylation of EGFR, and blocked the binding of the adaptor protein Grb2 to EGFR upon activation by EGF [ xref ]."

"In the present study the function of Ash/Grb-2 was investigated by microinjecting cells with an anti-Ash antibody. The antibody abolished both S phase entry and the reorganization of actin assembly to ruffle formation upon stimulation with epidermal growth factor (EGF) and platelet-derived growth factor (PDGF). On the other hand, anti-Ash antibody had no effect on S phase entry or actin stress fiber formation induced by either serum or lysophosphatidic acid. Since the induction of DNA synthesis, ruffle induction and stress fiber formation involve a function of Ras, Rac activation and Rho activation respectively, the findings strongly suggest that Ash plays a critical role in the signaling of both pathways downstream from growth factor receptors to Ras and Rac. Consistent with this, Ash co-precipitated with EGF receptor from EGF-stimulated cells."

"The temporal changes in the larger clusters were similar to those in the residence time of Grb2 on the plasma membrane, suggesting that large EGFR clusters extended the EGFR-Grb2 interaction upon EGF stimulation (Fig.  xref )."