Loading
The standard review of the receptor family behind many cancer drugs, explaining how growth factor receptors such as EGFR and HER2 switch on when they pair up, how mutations lock them on in cancer, and how inhibitors turn them off.
Lemmon and Schlessinger surveyed the 58 human receptor tyrosine kinases in 20 subfamilies, describing how ligand binding drives receptor dimerisation and trans-autophosphorylation, the structural diversity of activation mechanisms across families, and the intracellular pathways (RAS-MAPK, PI3K-AKT, PLC-gamma and STAT) that carry the signal. They explained how overexpression, amplification, point mutations and fusions deregulate these receptors in cancer and how antibodies and small-molecule kinase inhibitors exploit the same mechanisms, with resistance mutations as the predictable consequence.
Almost every targeted therapy on this site, from trastuzumab and EGFR inhibitors to ALK, MET, RET and FGFR drugs, acts on the receptors this review describes. It is the mechanistic background for understanding both why these drugs work and why resistance mutations arise.
Shares MET, ALK, Receptor tyrosine kinase activation, EGFR.
Shares MET, ALK, Receptor tyrosine kinase activation, EGFR.
Shares Signalling pathway, MET, EGFR.
Shares Receptor tyrosine kinase activation, EGFR, HER2.
Shares MET, ALK, Receptor tyrosine kinase activation, EGFR.
Shares Signalling pathway, EGFR.