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EGF phosphorylates EGFR on Y1069. 32 / 32
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sparser
"We next investigated the correlation between ROCK and EGF signaling, and found that exposure to Y27632 or knockdown of ROCK using siRNA strengthened the EGF-induced phosphorylation of EGFR at Tyr1045 and Tyr1068 (Figure xref )."

sparser
"EGF abundantly stimulated EGFR phosphorylation at Tyr992, Tyr1045, and Tyr1068, whereas amphiregulin did not stimulate phosphorylation at Tyr992 in either the NHBE or the BSMC."

reach
"EGF stimulates much greater phosphorylation of EGFR Tyr1045 than does AR."

reach
"EGF abundantly stimulated EGFR phosphorylation at Tyr1045, whereas amphiregulin did not, which is in agreement with the observations of Gilmore et al. 23 Phosphorylation of Tyr1045 creates a canonical[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

sparser
"Corroborating our data, in 32D/EGFR cells, EGF stimulates phosphorylation of EGFR Tyr1045 considerably more than amphiregulin."

reach
"EGF stimulates greater phosphorylation of EGFR Tyr1045 than does AREG."

reach
"Because EGF induced association between EGFR and Brk is EGFR Y1045 phosphorylation dependent (XREF_FIG), we next compared the levels of EGFR-Brk association in CHO cells expressing various combinations of EGFR constructs (wild type, EGFR-Y1045F, and EGFR-Y845F) and Brk constructs (Brk-Y447F and Brk-K219M) to further analyze the roles of Brk kinase activity and Brk induced EGFR Y845 phosphorylation in EGFR-Brk association (XREF_FIG)."

"Table 4. Quantification data from MRM-QTRAP analyses. Also see fig 4a. 2-fold cutoff; 32 min timepoint FC/ 0 min timepoint FC"

reach
"For example, EGF stimulates abundant EGFR phosphorylation at Tyr1045 whereas AR does not."

sparser
"Briefly, tyrosine 1045 of EGFR, which is phosphorylated by its ligand EGF and is the major docking site for c-Cbl , is not phosphorylated by treatment with HO."

sparser
"Published and unpublished data indicate that the functional difference appears to be due to the fact that EGF stimulates greater EGFR tyrosine phosphorylation at EGFR Tyr1045 than does AREG, resulting in greater EGFR coupling to the ubiquitin ligase c-Cbl and greater EGFR ubiquitination and more rapid EGFR turnover."

reach
"First, we demonstrated that the EGF induced EGFR-Brk association is EGFR Y1045 phosphorylation dependent."

reach
"Nonetheless, this hypothesis is supported by our observation that EGF stimulates much greater phosphorylation of EGFR Tyr1045 than does AR."

reach
"Indeed, EGF stimulates EGFR phosphorylation on Tyr1045 in 32D/EGFR cells, but AR does not (XREF_FIG)."

sparser
"EGF stimulates much greater EGFR tyrosine phosphorylation at Tyr 1045 and EGFR coupling to ubiquitination and down-regulation (via the ubiquitin ligase c-Cbl) than does AR [ xref , xref ]."

"To address this problem, we use quantitative mass spectrometry to analyze dynamic effects of HER2 overexpression on phosphotyrosine signaling in human mammary epithelial cells stimulated by epidermal growth factor (EGF) or heregulin (HRG). [This is from the 'Suplementary Table with Full Data Set\" (http://www.nature.com/msb/journal/v2/n1/suppinfo/msb4100094_S1.html). The cutoff used was a 2.5 fold or greater increase at any of the 5, 10 or 30 minute time points.]"

sparser
"EGF stimulates greater phosphorylation of EGFR Tyr1045 than does AREG."

reach
"We were not able to detect EGF mediated phosphorylation of other EGFR sites (Y992, Y1045, Y1068, Y1148, and Y1173) that were present on The RayBio (R) EGFR Phosphorylation Antibody Array."

"Under GO and cigarette smoke, Tyr-845 is hyperphosphorylated, and Tyr-1045 is not phosphorylated (Fig. 4A). With EGF exposure, Tyr-1045 is strongly phosphorylated, whereas Tyr-845 is phosphorylated to a much lesser extent (Fig. 4A)."

reach
"TSP1 and its EGF like repeats also increased phosphorylation of EGFR Tyr 845, Tyr 992, Tyr 1045, Tyr 1086, and Tyr 1173, activated phospholipase Cgamma, and increased cell migration."

sparser
"For example, EGF stimulates abundant EGFR phosphorylation at Tyr1045 whereas AR does not ( xref )."

"TABLE V Survey of cell signaling proteins that show a reaction to EGF ligand stimulation over a 180-min time course - 500ng/mL EGF results"

reach
"EGF also markedly and immediately induced the phosphorylation of EGFR at Tyr1045 and Tyr1068 at 0.5 min, reached a maximum within 1 min (data not shown), continued for up to 60 min, and decreased at 120 min after EGF-treatment."

reach
"In contrast, basal phosphorylation of EGFR at Tyr 1045 was minimal and was sharply increased by EGF treatment, consistent with induction of EGFR degradation."

reach
"EGF (10 ng/ml) caused the specific Tyr1045 phosphorylation of EGFR in all transfectants investigated."

sparser
"EGF abundantly stimulated EGFR phosphorylation at Tyr1045, whereas amphiregulin did not, which is in agreement with the observations of Gilmore et al. 23 Phosphorylation of Tyr1045 creates a canonica[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

reach
"Published and unpublished data indicate that the functional difference appears to be due to the fact that EGF stimulates greater EGFR tyrosine phosphorylation at EGFR Tyr1045 than does AREG, resulting in greater EGFR coupling to the ubiquitin ligase c-Cbl and greater EGFR ubiquitination and more rapid EGFR turnover."

reach
"The mechanism underlying the difference in the ability of EGF and AR to stimulate EGFR phosphorylation at Tyr1045 remains unknown."

reach
"EGF abundantly stimulated EGFR phosphorylation at Tyr992, Tyr1045, and Tyr1068, whereas amphiregulin did not stimulate phosphorylation at Tyr992 in either the NHBE or the BSMC."

sparser
"Specifically, EGF stimulates much greater phosphorylation of EGFR Tyr 1045 than does AR, thereby enabling EGF to stimulate greater EGFR coupling to the ubiquitin ligase c-Cbl than does AR."

sparser
"We next examined the effects of Y27632 on the EGF-induced phosphorylation of EGFR at Tyr1045 and Tyr1068 in Panc1, KP3 and AsPc1 cells."

reach
"EGF stimulation led to a robust phosphorylation of the EGFR on Y1045 and Y1068, the docking sites of c-Cbl and Grb2, respectively, in the controls, but phosphorylation on these sites was significantly reduced in the HER2 cells (XREF_FIG)."