Biochemical properties of the Drosophila EGF receptor homolog (DER) protein.
Antibodies recognizing the Drosophila EGF receptor homolog (DER) were used to define the biochemical properties of the protein. We show that DER is a glycosylated protein, with different processing patterns in Drosophila and mammalian cells, and confirm its localization in the plasma membrane with the predicted orientation. The receptor produced in transfected cells displays only a basal activity of in vivo tyrosine kinase autophosphorylation, providing a sensitive assay for ligands which may trigger DER. EGF and TGF alpha, which trigger the mammalian EGF receptor, did not increase the kinase activity of DER.
Zak
N B
NB
Department of Molecular Genetic and Virology, Weizmann Institute of Science, Rehovot, Israel.
Shilo
B Z
BZ
D000818:Animals; D000906:Antibodies; D002460:Cell Line; D004330:Drosophila / Q000235:genetics*; D029721:Drosophila Proteins; D066246:ErbB Receptors / Q000235:genetics*; D008970:Molecular Weight; D010766:Phosphorylation; D011494:Protein Kinases; D011505:Protein-Tyrosine Kinases / Q000378:metabolism*; D018010:Receptors, Invertebrate Peptide; D012689:Sequence Homology, Nucleic Acid; D014162:Transfection
D000906:Antibodies; D029721:Drosophila Proteins; D018010:Receptors, Invertebrate Peptide; D011494:Protein Kinases; C066532:Egfr protein, Drosophila; D066246:ErbB Receptors; D011505:Protein-Tyrosine Kinases