Human epidermal growth factor receptor dimerization (HER receptor dimerization)

Dimerization inhibition of HER family receptors refers to the pharmacological blockade of the physical association (homo- or hetero-dimerization) between members of the human epidermal growth factor receptor family—a group of four receptor tyrosine kinases: EGFR (HER1), HER2, HER3, and HER4. Ligand-induced or constitutive dimerization is necessary for activation of these receptors and resultant intracellular signaling that regulates cell proliferation, survival, and oncogenesis. Inhibiting the dimerization event (e.g., using the antibody pertuzumab at the HER2 dimerization interface) prevents transphosphorylation and downstream signaling, providing an effective therapeutic strategy in HER-driven cancers, most notably HER2-positive breast cancer[1][3]. While the modulation of dimerization is a mechanism rather than a specific protein or gene, drugs are developed to target this process by binding extracellular domains of HER receptors, thus blocking dimer formation and its pathological signaling consequences[1][2][3]. Caveat: The submitted "target" is a molecular process (dimerization inhibition) rather than a discrete gene/protein entity; for structured data, individual HER receptors (usually HER2, sometimes HER3 or HER1/EGTR) should be selected as canonical targets.

Other names

HER family dimerizationHER2 dimerizationHER2/HER3 dimerizationErbB family dimerizationEGFR family dimerization

Inhibition of receptor dimerization, thereby blocking downstream signaling; Blockade of ligand-induced dimerization; Disruption of potent HER2/HER3 heterodimer formation