Mechanism of desensitization of the epidermal growth factor receptor-tyrosine kinase

The intrinsic protein-tyrosine kinase activity of the epidermal growth factor (EGF) receptor is required for signal transduction. Increased protein-tyrosine kinase activity is observed following the binding of EGF to the receptor. However, signaling is rapidly desensitized during EGF treatment. We r...

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Bibliographic Details
Published in:The Journal of biological chemistry 1992-01, Vol.267 (2), p.1129-1140
Main Authors: Countaway, J L, Nairn, A C, Davis, R J
Format: Article
Language:English
Subjects:
protein-tyrosine kinase
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Summary:The intrinsic protein-tyrosine kinase activity of the epidermal growth factor (EGF) receptor is required for signal transduction. Increased protein-tyrosine kinase activity is observed following the binding of EGF to the receptor. However, signaling is rapidly desensitized during EGF treatment. We report that EGF receptors isolated from desensitized cells exhibit a lower protein-tyrosine kinase activity than EGF receptors isolated from control cells. The mechanism of desensitization of kinase activity can be accounted for in part, by the EGF-stimulated phosphorylation of the receptor at Ser super(1046/7), a substrate for the multifunctional calmodulin-dependent protein kinase II in vitro.
ISSN:0021-9258