IndraLab
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"In this assay, PLCγ1 was phosphorylated by the epidermal growth factor receptor (EGFR) and used as a substrate for PTPμ. xref shows that with increasing amounts of WT PTPμ there is a clear decrease in the tyrosine phosphorylation of PLCγ1 as well as a dramatic shift downward in the mobility of the protein, which is consistent with its dephosphorylation."
"In contrast, egf-induced tyrosine phosphorylation of plc-gamma 1 was rather small, indicating that tyrosine phosphorylation of plc-gamma 1 is not proportional to changes in plc activity. These results suggest that autophosphorylation of theegfr may induce a conformational change of its kinase domain which enhances its kinase activity with exogenous substrates and may induce association with phospholipase c-gamma by increasing its affinity to a domain containing tyr-771."
"We have identified the sites phosphorylated in vitro by epidermal growth factor (egf) receptor kinase in bovine brain phospholipase c-gamma (plc-gamma). They are tyrosine residues 472, 771, 783, and 1254. we propose, therefore, that the phosphorylation of plc-gamma by egf receptor kinase alters its interaction with putative inhibitory proteins and leads to its activation."
"We have identified the sites phosphorylated in vitro by epidermal growth factor (egf) receptor kinase in bovine brain phospholipase c-gamma (plc-gamma). They are tyrosine residues 472, 771, 783, and 1254. we propose, therefore, that the phosphorylation of plc-gamma by egf receptor kinase alters its interaction with putative inhibitory proteins and leads to its activation."
"Despite extensive overlap in the molecules recruited to the active receptors, there is some preferential modulation of signalling pathways. Tumour cells that express EGFR with kinase-domain mutations preferentially activate the pro-survival PI3K?AKT and signal transducer and activator of transcription (STAT) pathways67. Although EGFR has no consensus sequence for the p85 adaptor subunit of PI3K, it couples to this pathway through GAB1, which binds growth-factorreceptor- bound protein 2 (GRB2)."
"Despite extensive overlap in the molecules recruited to the active receptors, there is some preferential modulation of signalling pathways. Tumour cells that express EGFR with kinase-domain mutations preferentially activate the pro-survival PI3K?AKT and signal transducer and activator of transcription (STAT) pathways67. Although EGFR has no consensus sequence for the p85 adaptor subunit of PI3K, it couples to this pathway through GAB1, which binds growth-factorreceptor- bound protein 2 (GRB2)."
"From Fig. 4: Using the same time and dose strategies as before, a mean 6.2-fold induction of PLC{gamma} phosphorylation was observed following radiation treatment (Fig. 4). Increases in phosphorylation of Shc family members were observed following irradiation; the mean -fold changes (n = 3) were 2.3, 3.0, and 3.5 for the 66-, 52-, and 46-kDa isoforms, respectively. For both PLC{gamma} and Shc, EGF at 10 ng/ml induced a significantly greater increase in phosphorylation than IR (p < 0.05). Pretreatment of cells with 500 nM AG1478, a specific inhibitor of EGFR Tyr phosphorylation (29), abolished the radiation- and EGF-induced activation of both PLC{gamma} and Shc in A431 cells."