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- W2990295477 abstract "4827 A hallmark of glioblastoma multiforme (GBM) is the amplification and rearrangement of the epidermal growth factor receptor. One of the more frequently occurring rearrangements, termed variant III (vIII), has an in-frame deletion in the extracellular domain. EGFRvIII is constitutively active and subsequently activates several other downstream signaling pathways. Using EGFR and phospho-EGFR specific antibodies, we demonstrate that EGFRvIII is phosphorylated more extensively on tyrosine than the wildtype receptor. We also show, using transcriptional activation assays, that enforced expression of EGFRvIII results in the activation of the transcription factor STAT3 to a greater extent than the wildtype receptor. Using STAT3 carrying an electrochemiluminescent label, we quantified the interaction between immobilized EGFR and STAT3. We studied a panel of receptors containing single or combinations of mutations at the receptor’s known autophosphorylation sites and determined that tyrosine 1068 is the primary association site for STAT3 on EGFR. The importance of this residue in STAT3 signaling was confirmed independently using a STAT3 transcriptional activity assay and receptors containing or lacking tyrosine at position 1068. This panel of mutants will allow us to continue to characterize the role of STAT3 activity and that of other pathways on EGFR-initiated signaling pathways." @default.
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- W2990295477 date "2006-04-15" @default.
- W2990295477 modified "2023-09-28" @default.
- W2990295477 title "Activation of STAT3 by EGFR variant III: Tyrosine residue 1068 is the primary STAT3 docking site on EGFR" @default.
- W2990295477 hasPublicationYear "2006" @default.
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