◀ Back to EGFR

EGFR — NCOA3

Text-mined interactions from Literome

Lahusen et al., Cancer Res 2007 (Breast Neoplasms) : Further analysis revealed that the depletion of AIB1 reduced tyrosine phosphorylation of EGFR at multiple residues both at autophosphorylation and Src kinase phosphorylation sites
Long et al., Mol Cell 2010 (Lung Neoplasms...) : SRC-3Delta4 mediates the interaction of EGFR with FAK to promote cell migration
Deb et al., Am J Physiol Cell Physiol 2011 : Collectively, these data suggest that 1 ) Pnck induces ligand independent EGFR degradation most likely through perturbation of Hsp90 chaperone activity due to Hsp90 phosphorylation, 2 ) EGFR degradation is coupled to proteasomal degradation of Pnck, and 3 ) modulation of basal MAP kinase activity, p21/Cip-1/Waf-1 expression, and cellular growth by Pnck is independent of Pnck induced ligand independent EGFR degradation
Skarpen et al., Exp Cell Res 1998 : Consistently, we found more rapid dephosphorylation of the EGFR and less induction of p21/CIP1 by TGFalpha than by EGF ... When surface bound TGFalpha was removed by acid stripping and endosomal pH was neutralized with bafilomycin A1, TGFalpha stimulated EGFR tyrosine phosphorylation, induced p21/CIP1 , and inhibited DNA synthesis ... This strongly suggests that p21/CIP1 can be induced by endocytosed, activated EGFR and that endocytosed EGFR can affect cell growth