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The Role of Carbohydrate as a Post-Translational Modification of the Receptor for Epidermal Growth Factor

  • Ann M. Soderquist
  • Gordon Todderud
  • Graham Carpenter
Part of the Advances in Experimental Medicine and Biology book series (NATO ASI F, volume 231)

Abstract

The receptor for EGF is an integral membrane protein that mediates the mitogenic response of target cells to EGF and EGF-like polypeptides (1). The EGF receptor has been purified from cultured human tumor cells (2,3) and mouse liver (4). The receptor is a glycoprotein having an estimated molecular mass of approximately 170,000 daltons and no subunit structure. In addition to the N-linked oligosaccharide chains, the EGF receptor is also modified post-translationally by phosphate on serine, threonine, and tyrosine residues and extensive disulfide bond arrangement is predicted. In addition to the molecule’s ligand binding capacity, the receptor acts as an allosteric enzyme; it contains a tyrosine-specific protein kinase activity that is activated by the binding of EGF (5,6). However, substrates of this receptor-kinase that are physiologically relevant to mito-genesis have not yet been identified. The focus of this article will be on the glycosylation of the EGF receptor during the biosynthesis of this molecule.

Keywords

Epidermal Growth Factor Receptor Human Epidermal Growth Factor Receptor Epidermal Growth Factor Receptor Kinase Mature Receptor Autophosphorylation Site 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1988

Authors and Affiliations

  • Ann M. Soderquist
    • 1
  • Gordon Todderud
    • 1
  • Graham Carpenter
    • 1
  1. 1.Department of BiochemistryVanderbilt University School of MedicineNashvilleUSA

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