ErbB receptors: directing key signaling networks throughout life.
@article{Holbro2004ErbBRD, title={ErbB receptors: directing key signaling networks throughout life.}, author={Thomas Holbro and Nancy E Hynes}, journal={Annual review of pharmacology and toxicology}, year={2004}, volume={44}, pages={ 195-217 } }
The epidermal growth factor (EGF)-related peptides bind the ErbB receptors, inducing the formation of different homo- and heterodimers. Receptor dimerization promotes activation of the intrinsic kinase, leading to phosphorylation of specific tyrosines located in the ErbB's cytoplasmic region. These phosphorylated residues serve as docking sites for a variety of signaling molecules whose recruitment stimulates intracellular signaling cascades, which ultimately control diverse genetic programs…
618 Citations
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Alternative endocytic trafficking of ligand-ErbB complexes may tune and diversify signal transduction by EGF family ligands.
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Several characteristics of hormone‐receptor interactions and receptor coupling that contribute to specificity are discussed and there are three distinct functional groups of EGF family hormones.
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The role of ErbB receptors as normal signal transducers and their contribution to the process of malignant transformation during tumor development are concentrated on.
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The results indicate that ErbB4 activation by growth factors is not generic and suggest that individual Erb B receptors can discriminate between different EGF-like ligands within the context of a single receptor dimer.
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It is shown that mice homozygous for the kinase-dead erbB-2 allele die at midgestation and display the same spectrum of embryonic defects seen in erb B-2 knockout mutants, suggesting that the catalytic activity of ErbB/Neu is essential for normal embryonic development.
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