Post-translational processing of the epidermal growth factor receptor. Glycosylation-dependent acquisition of ligand-binding capacity.

Abstract

The post-translational processing of the epidermal growth factor receptor in human A431 epidermoid carcinoma cells has been investigated. By employing the affinity matrix epidermal growth factor Affi-Gel in conjunction with immunoprecipitation, it has been demonstrated that core oligosaccharide addition is essential for the acquisition of epidermal growth factor-binding activity. Furthermore, the initial 160-kDa translation product was observed to undergo a processing step by which ligand-binding activity was acquired with a half-time of approximately 30 min while exhibiting no apparent change in mobility on sodium dodecyl sulfate-polyacrylamide gels. This was shown not to involve the conversion of high-mannose chains to complex chains which have been capped with fucose and sialic acid. Possible explanations for this activation in terms of translocation of intermediates and/or formation of disulfide bonds are discussed.

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@article{Slieker1985PosttranslationalPO, title={Post-translational processing of the epidermal growth factor receptor. Glycosylation-dependent acquisition of ligand-binding capacity.}, author={Lawrence J Slieker and Melissa D. Lane}, journal={The Journal of biological chemistry}, year={1985}, volume={260 2}, pages={687-90} }