title: Complete canthi removal reveals that forces from the amnioserosa alone are sufficient to drive dorsal closure in Drosophila.
abstract: Drosophila's dorsal closure provides an excellent model system with which to analyze biomechanical processes during morphogenesis. During native closure, the amnioserosa, flanked by two lateral epidermal sheets, forms an eye-shaped opening with canthi at each corner. The dynamics of amnioserosa cells and actomyosin purse strings in the leading edges of epidermal cells promote closure, whereas the bulk of the lateral epidermis opposes closure. Canthi maintain purse string curvature (necessary for their dorsalward forces), and zipping at the canthi shortens leading edges, ensuring a continuous epithelium at closure completion. We investigated the requirement for intact canthi during closure with laser dissection approaches. Dissection of one or both canthi resulted in tissue recoil and flattening of each purse string. After recoil and a temporary pause, closure resumed at approximately native rates until slowing near the completion of closure. Thus the amnioserosa alone can drive closure after dissection of one or both canthi, requiring neither substantial purse string curvature nor zipping during the bulk of closure. How the embryo coordinates multiple, large forces (each of which is orders of magnitude greater than the net force) during native closure and is also resilient to multiple perturbations are key extant questions.
authors.affiliation: Department of Biology, Duke University, Durham, NC 27708.
authors.forename: Adrienne R
authors.initials: AR
authors.lastname: Wells
authors.affiliation: Department of Biology, Duke University, Durham, NC 27708.
authors.forename: Roger S
authors.initials: RS
authors.lastname: Zou
authors.affiliation: Department of Biology, Duke University, Durham, NC 27708.
authors.forename: U Serdar
authors.initials: US
authors.lastname: Tulu
authors.affiliation: Department of Physics, Duke University, Durham, NC 27708.
authors.forename: Adam C
authors.initials: AC
authors.lastname: Sokolow
authors.affiliation: Department of Biology, Duke University, Durham, NC 27708.
authors.forename: Janice M
authors.initials: JM
authors.lastname: Crawford
authors.affiliation: Department of Physics, Duke University, Durham, NC 27708.
authors.forename: Glenn S
authors.initials: GS
authors.lastname: Edwards
authors.affiliation: Department of Biology, Duke University, Durham, NC 27708 dkiehart@duke.edu.
authors.forename: Daniel P
authors.initials: DP
authors.lastname: Kiehart
mesh_terms: D000205:Actomyosin / Q000378:metabolism; D000825:Animal Structures / Q000196:embryology* / Q000378:metabolism / Q000648:ultrastructure; D000818:Animals; D001696:Biomechanical Phenomena; D004331:Drosophila melanogaster / Q000166:cytology / Q000196:embryology* / Q000378:metabolism; D004625:Embryo, Nonmammalian; D047108:Embryonic Development; D004817:Epidermis / Q000196:embryology / Q000378:metabolism / Q000648:ultrastructure; D004847:Epithelial Cells / Q000166:cytology / Q000378:metabolism; D061346:Laser Capture Microdissection; D040542:Mechanotransduction, Cellular; D009024:Morphogenesis; D012704:Serous Membrane / Q000378:metabolism / Q000648:ultrastructure*
chemical_list: D000205:Actomyosin