title: Phantom, a cytochrome P450 enzyme essential for ecdysone biosynthesis, plays a critical role in the control of border cell migration in Drosophila.
abstract: The border cells of Drosophila are a model system for coordinated cell migration. Ecdysone signaling has been shown to act as the timing signal to initiate the migration process. Here we find that mutations in phantom (phm), encoding an enzyme in the ecdysone biosynthesis pathway, block border cell migration when the entire follicular epithelium of an egg chamber is mutant, even when the associated germline cells (nurse cells and oocyte) are wild-type. Conversely, mutant germline cells survive and do not affect border cell migration, as long as the surrounding follicle cells are wild-type. Interestingly, even small patches of wild-type follicle cells in a mosaic epithelium are sufficient to allow the production of above-threshold levels of ecdysone to promote border cell migration. The same phenotype is observed with mutations in shade (shd), encoding the last enzyme in the pathway that converts ecdysone to the active 20-hydroxyecdysone. Administration of high 20-hydroxyecdysone titers in the medium can also rescue the border cell migration phenotype in cultured egg chambers with an entirely phm mutant follicular epithelium. These results indicate that in normal oogenesis, the follicle cell epithelium of each individual egg chamber must supply sufficient ecdysone precursors, leading ultimately to high enough levels of mature 20-hydroxyecdysone to the border cells to initiate their migration. Neither the germline, nor the neighboring egg chambers, nor the surrounding hemolymph appear to provide threshold amounts of 20-hydroxyecdysone to do so. This "egg chamber autonomous" ecdysone synthesis constitutes a useful way to regulate the individual maturation of the asynchronous egg chambers present in the Drosophila ovary.
authors.affiliation: Howard Hughes Medical Institute, Department of Molecular Biology, Princeton University, Princeton, New Jersey, United States.
authors.forename: Elena
authors.initials: E
authors.lastname: Domanitskaya
authors.affiliation: Howard Hughes Medical Institute, Department of Molecular Biology, Princeton University, Princeton, New Jersey, United States.
authors.forename: Lauren
authors.initials: L
authors.lastname: Anllo
authors.affiliation: Howard Hughes Medical Institute, Department of Molecular Biology, Princeton University, Princeton, New Jersey, United States. Electronic address: schupbac@princeton.edu.
authors.forename: Trudi
authors.initials: T
authors.lastname: Schüpbach
mesh_terms: D000818:Animals; D002465:Cell Movement / Q000502:physiology*; D004330:Drosophila / Q000196:embryology* / Q000201:enzymology*; D029721:Drosophila Proteins / Q000235:genetics / Q000378:metabolism*; D004440:Ecdysone / Q000096:biosynthesis* / Q000235:genetics; D004441:Ecdysterone / Q000378:metabolism*; D008856:Microscopy, Fluorescence; D006899:Mixed Function Oxygenases / Q000235:genetics / Q000378:metabolism*; D009154:Mutation / Q000235:genetics
chemical_list: D029721:Drosophila Proteins; D004440:Ecdysone; D004441:Ecdysterone; D006899:Mixed Function Oxygenases; C496261:Phm protein, Drosophila
keywords: Border cell migration; Drosophila; Ecdysone biosynthesis; Oogenesis; Phantom (phm); Shade (shd)