EGFR biology

EGFR biology. Ligand binding to domains I and III of the EGFR expose the dimerization loop in domain II and induce receptor homo- or hetero-dimerization. This process activates the intrinsic tyrosine kinase activity of the EGFR and leads to the phosphorylation of specific tyrosines on the cytoplasmic tails of the receptor pair. These phospho-tyrosines serve to recruit specific effector molecules containing SH2 or PTB domains. These effector molecules recruit and induce various signaling pathways including the PI3K/AKT (A), RAS/MAPK (A), PLCγ/PKC (B) and STAT (B) pathways. In addition, a less appreciated pathway, the nuclear EGFR signaling pathway (C), is initiated upon ligand binding and induces EGFR translocation to the nucleus where it behaves as a co-transcriptional activator regulating key genes such as Cox2, iNOS, B-myb, Aurora kinase A and Cyclin D1.

Publication

Molecular mechanisms of resistance to the EGFR monoclonal antibody cetuximab. (2011) Toni M Brand, et al. Cancer Biol Ther. 2011 May 1;11(9):777-792. Figure: F1. All organisms Homo sapiens Drosophila melanogaster

Disease mentions