title: Ectopic activation of torpedo/Egfr, a Drosophila receptor tyrosine kinase, dorsalizes both the eggshell and the embryo.
abstract: The Drosophila gene torpedo/Egfr (top/Egfr) encodes a homolog of the vertebrate Epidermal Growth Factor receptor. This receptor is required several times during the life cycle of the fly for the transmisson of developmental cues. During oogenesis, Top/Egfr activation is required for the establishment of the dorsal/ventral axis of the egg and the embryo. To examine how ectopic Top/Egfr activation affects cell fate determination, we constructed an activated version of the protein. Expression of this activated form (lambda top) in the follicle cells of the ovary induces dorsal cell fates in both the follicular epithelium and the embryo. Different levels of expression resulted in different dorsal follicle cell fates. These dorsal cell fates were expanded in the anterior, but not the posterior, of the egg, even in cases where all the follicle cells covering the oocyte expressed lambda top. The expression of genes known to respond to top/Egfr activation, argos (aos), kekkon1 (kek 1) and rhomboid (rho), was also expanded in the presence of the lambda top construct. When lambda top was expressed in all the follicle cells covering the oocyte, kek 1 and argos expression was induced in follicle cells all along the anterior/posterior axis of the egg chamber. In contrast, rho RNA expression was only activated in the anterior of the egg chamber. These data indicate that the response to Top/Egfr signaling is regulated by an anterior/posterior prepattern in the follicle cells. Expression of lambda top in the entire follicular epithelium resulted in an embryo dorsalized along the entire anterior/posterior axis. Expression of lambda top in anterior or posterior subpopulations of follicle cells resulted in regionally autonomous dorsalization of the embryos. This result indicates that subpopulations of follicle cells along the anterior/posterior axis can respond to Top/Egfr activation independently of one another.
authors.affiliation: Howard Hughes Medical Institute, Department of Molecular Biology, Princeton University, NJ 08544, USA.
authors.forename: A M
authors.initials: AM
authors.lastname: Queenan
authors.forename: A
authors.initials: A
authors.lastname: Ghabrial
authors.forename: T
authors.initials: T
authors.lastname: Schüpbach
mesh_terms: D000818:Animals; D019521:Body Patterning / Q000235:genetics; D016764:Cell Polarity; D003433:Crosses, Genetic; D019281:Dimerization; D004330:Drosophila / Q000196:embryology* / Q000235:genetics; D029721:Drosophila Proteins; D004528:Egg Shell / Q000502:physiology; D004625:Embryo, Nonmammalian / Q000502:physiology*; D066246:ErbB Receptors / Q000096:biosynthesis*; D005123:Eye / Q000166:cytology / Q000196:embryology / Q000648:ultrastructure; D005260:Female; D018507:Gene Expression Regulation, Developmental; D008855:Microscopy, Electron, Scanning; D010053:Ovary / Q000502:physiology; D010063:Ovum / Q000502:physiology; D011494:Protein Kinases; D018010:Receptors, Invertebrate Peptide / Q000096:biosynthesis*; D014714:Vertebrates; D014921:Wings, Animal / Q000166:cytology / Q000196:embryology / Q000254:growth & development
chemical_list: D029721:Drosophila Proteins; D018010:Receptors, Invertebrate Peptide; D011494:Protein Kinases; C066532:Egfr protein, Drosophila; D066246:ErbB Receptors