Role of conformational alteration in the epidermal growth factor receptor (EGFR) function.
This mini-review addresses the effect of glycosylation and phosphorylation on the conformational alterations of the epidermal growth factor receptor (EGFR). Based on studies with full-length and truncated EGFRs, we propose a model to suggest that receptor-receptor self-association, which occurs in the truncated receptor and depends on core glycosylation, is prevented in intact receptor by a certain extracellular domain and that the function of the ligand is to remove the negative constraint. We also propose, based on works with a conformation-specific antibody directed to an unphosphorylated peptide, that the interactions among negatively charged phosphotyrosine residues in the receptor molecule result in bringing two epitopes separated by a long stretch of amino acids close to each other to form an antibody-binding site. The implications of these posttranslational modifications on receptor functions are also discussed in this article.
Bishayee
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Pathology and Laboratory Medicine, UMDNJ-New Jersey Medical School, Newark, NJ 07103, USA. bishayee@umdnj.edu
D000906:Antibodies / Q000276:immunology; D066246:ErbB Receptors / Q000737:chemistry* / Q000276:immunology / Q000378:metabolism / Q000502:physiology; D006031:Glycosylation; D006801:Humans; D010766:Phosphorylation; D011487:Protein Conformation
D000906:Antibodies; D066246:ErbB Receptors