ErbB receptors, their ligands, and the consequences of their activation and inhibition in the myocardium

Journal of Molecular and Cellular Cardiology
Stephen J FullerPeter H Sugden

Abstract

The epidermal growth factor (EGF) receptor (or ErbB1) and the related ErbB4 are transmembrane receptor protein tyrosine kinases which bind extracellular ligands of the EGF family. ErbB2 and ErbB3 are "co-receptors" structurally related to ErbB1/ErbB4, but ErbB2 is an "orphan" receptor and ErbB3 lacks tyrosine kinase activity. However, both are important in transmembrane signalling. All ErbB receptors/ligands are intimately involved in the regulation of cell growth, differentiation and survival, and their dysregulation contributes to some human malignancies. After extracellular ligand binding, receptor dimerisation and transautophosphorylation of intracellular C-terminal tyrosine residues, they bind signalling proteins which recognise specific tyrosine-phosphorylated motifs. This leads to activation of multiple signalling pathways, notably the extracellular signal-regulated kinase 1/2 (ERK1/2) cascade and the phosphoinositide 3-kinase (PI3K)/protein kinase B [PKB/(Akt)] pathway. In heart, targeted deletion of ErbB2, ErbB3, ErbB4 and some ErbB receptor extracellular ligands leads to embryonic lethality resulting from cardiovascular defects. ErbB receptor ligands improve cardiac myocyte viability and are hypertrophic, partly becau...Continue Reading

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