EGF domain swap converts a drosophila EGF receptor activator into an inhibitor
| Autor: | Amanda Simcox, Timothy Donaldson, Ben-Zion Shilo, Ronen Schweitzer, Bruce C. Schnepp, Gary Grumbling, Stephen Ostrowski |
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| Rok vydání: | 1998 |
| Předmět: |
Recombinant Fusion Proteins
Molecular Sequence Data Nerve Tissue Proteins Biology Eye Research Communication Epidermal growth factor Genetics Animals Drosophila Proteins Wings Animal Amino Acid Sequence Receptor Eye Proteins Peptide sequence Neuregulins Epidermal Growth Factor Sequence Homology Amino Acid Activator (genetics) Membrane Proteins Molecular biology In vitro ErbB Receptors Phenotype Membrane protein Neuregulin Insect Proteins Drosophila Genetic Engineering Sequence Alignment Drosophila Protein hormones hormone substitutes and hormone antagonists Developmental Biology |
| Zdroj: | Genesdevelopment. 12(7) |
| ISSN: | 0890-9369 |
| Popis: | In Drosophila the function of the epidermal growth factor (EGF) receptor is modulated zygotically by three EGF-like proteins: Spitz (Spi), which is a potent activator; Vein (Vn), which is a moderate activator; and Argos (Aos), which is an inhibitor. Chimeric molecules were constructed in which the EGF domain of Vn was swapped with the EGF domain from each factor. The modified Vn proteins behaved both in vitro and in vivo with properties characteristic of the factor from which the EGF domain was derived. These results demonstrate that the EGF domain is the key determinant that gives DER inhibitors and activators their distinct properties. |
| Databáze: | OpenAIRE |
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