Abstract
There are four members of the EGFR family: EGFR, erbB2, erbB3 and erbB4. These receptors form ligand-activated oligomers which regulate intracellular processes via an oligomeric tyrosine kinase scaffold. The receptors are activated when the extracellular domain undergoes a conformational change which facilitates either homo- or hetero-oligomerization with other family members. The absence of one EGFR family member leads to embryonic or early post-natal death due to implantation, central nervous system or cardiac defects. Many mouse models of defective or deficient EGFR family members are available for studying physiology and/or pathology of EGFR family members. Sophisticated antibody and kinase inhibitors which target different family members have been designed, produced. EGFR and erbB2 are frequently activated, over expressed or mutated in many common cancers and the antagonists and/or inhibitors of EGFR and/or erbB2 signalling have already been shown to have therapeutic benefits for cancer patients.
Notes
†The EGFR family members regulate the production, survival, movement, and shape of many embryonic and adult cell types. Signalling from three of the family members EGFR, erbB3 and erbB4) are regulated by ligand dependent oligomerization and fourth, erbB2, by oligomerization with ligated forms of the other family members. Three of the family members (EGFR, erbB2 and erbB4) signal via activated tyrosine kinase scaffolds, the fourth, erbB3, by ligand induced oligomerization and activation of the other family members.