Abstract
The notable amino acid homology among mammalian growth factor receptors with tyrosine-specific protein kinase activity has led to speculation that these receptors derived from a common evolutionary precursor. We report the identification of a novel growth factor receptor from Drosophila cell cultures that has dual binding specificity for both insulin and epidermal growth factor (EGF). This 100-kDa protein is also related antigenically to the mammalian receptors for EGF and possibly insulin but may not correspond to the mammalian counterpart of either receptor in Drosophila. The Drosophila protein is recognized by antisera directed against the mammalian receptor for EGF in immunoblot hybridizations. It can be affinity labeled with either 125I-labeled insulin or 125I-labeled EGF after immunoprecipitation with anti-EGF receptor antiserum. Excess unlabeled EGF or insulin will block the affinity labeling with either growth factor, suggesting that both EGF and insulin share a common binding site on the 100-kDa Drosophila receptor. This Drosophila protein, therefore, may be closely related to an evolutionary precursor of the mammalian receptors for insulin and EGF.
MeSH Terms
Affinity Labels
Animals
Biological Evolution
Cell Line
Cross Reactions
Drosophila melanogaster/analysis,genetics
ErbB Receptors
Growth Substances/metabolism
Immunologic Techniques
Membrane Proteins/immunology,metabolism
Molecular Weight
Receptor, Insulin/immunology,metabolism
Receptors, Cell Surface/immunology,metabolism
Chemicals
Affinity Labels
Growth Substances
Membrane Proteins
Receptors, Cell Surface
ErbB Receptors
Receptor, Insulin
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Thompson K L
Decker S J
Rosner M R
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