title: Drosophila laminins act as key regulators of basement membrane assembly and morphogenesis.
abstract: Laminins are heterotrimeric molecules found in all basement membranes. In mammals, they have been involved in diverse developmental processes, from gastrulation to tissue maintenance. The Drosophila genome encodes two laminin alpha chains, one beta and one Gamma, which form two distinct laminin trimers. So far, only mutations affecting one or other trimer have been analysed. In order to study embryonic development in the complete absence of laminins, we mutated the gene encoding the sole laminin beta chain in Drosophila, LanB1, so that no trimers can be made. We show that LanB1 mutant embryos develop until the end of embryogenesis. Electron microscopy analysis of mutant embryos reveals that the basement membranes are absent and the remaining extracellular material appears disorganised and diffuse. Accordingly, abnormal accumulation of major basement membrane components, such as Collagen IV and Perlecan, is observed in mutant tissues. In addition, we show that elimination of LanB1 prevents the normal morphogenesis of most organs and tissues, including the gut, trachea, muscles and nervous system. In spite of the above structural roles for laminins, our results unravel novel functions in cell adhesion, migration and rearrangement. We propose that while an early function of laminins in gastrulation is not conserved in Drosophila and mammals, their function in basement membrane assembly and organogenesis seems to be maintained throughout evolution.
authors.affiliation: Centro Andaluz de Biología de Desarrollo (CABD), Univ. Pablo de Olavide-CSIC, 41013 Sevilla, Spain. mdmarber@upo.es
authors.forename: Jose M
authors.initials: JM
authors.lastname: Urbano
authors.forename: Catherine N
authors.initials: CN
authors.lastname: Torgler
authors.forename: Cristina
authors.initials: C
authors.lastname: Molnar
authors.forename: Ulrich
authors.initials: U
authors.lastname: Tepass
authors.forename: Ana
authors.initials: A
authors.lastname: López-Varea
authors.forename: Nicholas H
authors.initials: NH
authors.lastname: Brown
authors.forename: Jose F
authors.initials: JF
authors.lastname: de Celis
authors.forename: Maria D
authors.initials: MD
authors.lastname: Martín-Bermudo
mesh_terms: D000818:Animals; D001485:Basement Membrane / Q000196:embryology / Q000502:physiology*; D002448:Cell Adhesion; D002465:Cell Movement; D024141:Collagen Type IV / Q000378:metabolism; D004330:Drosophila / Q000196:embryology* / Q000502:physiology; D029721:Drosophila Proteins / Q000502:physiology*; D004625:Embryo, Nonmammalian / Q000502:physiology*; D019812:Heparan Sulfate Proteoglycans / Q000378:metabolism; D007797:Laminin / Q000502:physiology*; D009024:Morphogenesis / Q000235:genetics; D009154:Mutation; D009928:Organ Specificity
chemical_list: D024141:Collagen Type IV; D029721:Drosophila Proteins; D019812:Heparan Sulfate Proteoglycans; D007797:Laminin; C546979:LanB1 protein, Drosophila; C071927:perlecan