title: Somatic insulin signaling regulates a germline starvation response in Drosophila egg chambers.
abstract: Egg chambers from starved Drosophila females contain large aggregates of processing (P) bodies and cortically enriched microtubules. As this response to starvation is rapidly reversed upon re-feeding females or culturing egg chambers with exogenous bovine insulin, we examined the role of endogenous insulin signaling in mediating the starvation response. We found that systemic Drosophila insulin-like peptides (dILPs) activate the insulin pathway in follicle cells, which then regulate both microtubule and P body organization in the underlying germline cells. This organization is modulated by the motor proteins Dynein and Kinesin. Dynein activity is required for microtubule and P body organization during starvation, while Kinesin activity is required during nutrient-rich conditions. Blocking the ability of egg chambers to form P body aggregates in response to starvation correlated with reduced progeny survival. These data suggest a potential mechanism to maximize fecundity even during periods of poor nutrient availability, by mounting a protective response in immature egg chambers.
authors.affiliation: Department of Cell Biology, Yale University School of Medicine, 333 Cedar Street, New Haven, CT 06520, United States.
authors.forename: K Mahala
authors.initials: KM
authors.lastname: Burn
authors.affiliation: Graduate School of Life and Environmental Sciences, University of Tsukuba, Seinou-tou D301, Tennoudai 1-1-1, Tsukuba,, Ibaraki 305-8572, Japan.
authors.forename: Yuko
authors.initials: Y
authors.lastname: Shimada
authors.affiliation: Department of Genetics, Yale University School of Medicine, 333 Cedar Street, New Haven, CT 06520, United States.
authors.forename: Kathleen
authors.initials: K
authors.lastname: Ayers
authors.affiliation: Department of Genetics, Yale University School of Medicine, 333 Cedar Street, New Haven, CT 06520, United States.
authors.forename: Soumya
authors.initials: S
authors.lastname: Vemuganti
authors.affiliation: Department of Genetics, Yale University School of Medicine, 333 Cedar Street, New Haven, CT 06520, United States.
authors.forename: Feiyue
authors.initials: F
authors.lastname: Lu
authors.affiliation: Department of Genetics, Yale University School of Medicine, 333 Cedar Street, New Haven, CT 06520, United States.
authors.forename: Andrew M
authors.initials: AM
authors.lastname: Hudson
authors.affiliation: Department of Cell Biology, Yale University School of Medicine, 333 Cedar Street, New Haven, CT 06520, United States; Department of Genetics, Yale University School of Medicine, 333 Cedar Street, New Haven, CT 06520, United States; Department of Molecular, Cellular and Developmental Biology, Yale University, 260 Prospect Street, New Haven, CT 06510, United States. Electronic address: lynn.cooley@yale.edu.
authors.forename: Lynn
authors.initials: L
authors.lastname: Cooley
mesh_terms: D000818:Animals; D017209:Apoptosis; D002417:Cattle; D022083:Cytoplasmic Structures / Q000378:metabolism; D029721:Drosophila Proteins / Q000378:metabolism; D004331:Drosophila melanogaster / Q000166:cytology* / Q000196:embryology / Q000378:metabolism*; D004625:Embryo, Nonmammalian / Q000378:metabolism; D005260:Female; D005502:Food; D005854:Germ Cells / Q000378:metabolism*; D007328:Insulin / Q000378:metabolism*; D008870:Microtubules / Q000378:metabolism; D008954:Models, Biological; D009865:Oocytes / Q000378:metabolism; D006080:Ovarian Follicle / Q000166:cytology / Q000378:metabolism; D010063:Ovum / Q000166:cytology* / Q000378:metabolism; D010455:Peptides / Q000378:metabolism; D020871:RNA Stability; D012333:RNA, Messenger / Q000235:genetics / Q000378:metabolism; D012270:Ribosomes / Q000378:metabolism; D015398:Signal Transduction; D058570:TOR Serine-Threonine Kinases / Q000378:metabolism
chemical_list: D029721:Drosophila Proteins; D007328:Insulin; D010455:Peptides; D012333:RNA, Messenger; C416303:target of rapamycin protein, Drosophila; D058570:TOR Serine-Threonine Kinases
keywords: Dynein; Insulin; Kinesin; Microtubule; Oogenesis; P body