IndraLab

Statements


EGFR phosphorylates SRC. 5 / 5
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"EGFRvIII increased SFK phosphorylation in U87MG cells and sensitized them to dasatinib in matrigel migration assays (XREF_FIG)."

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"For example, EGFRvIII phosphorylates SFKs, which further activate dedicator of cytokinesis 1 (DOCK1). xref DOCK1 plays critical roles in mediating cell growth and migration, contributing to the pro-tumorigenic function of EGFRvIII. xref , xref EGFRvIII can also increase phosphorylation of DOCK1 through PKA. xref EGFRvIII forms a complex with the cytokine receptor OSMR, which regulates the EGFRvIII-STAT3 signaling axis. xref Additionally, SFK activation promotes mitochondrial localization of EGFRvIII, and increases cell survival under low glucose conditions. xref Moreover, EGFRvIII activates hepatocyte growth factor receptor (MET), which in-turn drives STAT3. xref , xref EGFRvIII also activates c-SRC, which promotes secretion of vascular endothelial growth factor (VEGF) and angiogenesis. xref Phosphorylation of these kinases further activates downstream signaling pathways and contributes to tumor progression."

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"These findings support the idea that Src and the EGF receptor cooperate in a regulated fashion to direct the phosphorylation of both Src- and receptor specific targets."

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"For example, EGFRvIII phosphorylates SFKs, which further activate dedicator of cytokinesis 1 (DOCK1)."

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"The EGFR dependent NSCLC cell lines HCC827 and H3255 had increased phosphorylation of SFKs, and treatment of these cells with an SFK inhibitor (PP1 or SKI-606) induced apoptosis."
Kinase-active EGFR leads to the phosphorylation of SRC. 1 / 1
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"The EGFR-dependent NSCLC cell lines HCC827 and H3255 had increased phosphorylation of SFKs, and treatment of these cells with an SFK inhibitor (PP1 or SKI-606) induced apoptosis."