title: The Ly6 protein coiled is required for septate junction and blood brain barrier organisation in Drosophila.
abstract: BACKGROUND
  Genetic analysis of the Drosophila septate junctions has greatly contributed to our understanding of the mechanisms controlling the assembly of these adhesion structures, which bear strong similarities with the vertebrate tight junctions and the paranodal septate junctions. These adhesion complexes share conserved molecular components and have a common function: the formation of paracellular barriers restraining the diffusion of solutes through epithelial and glial envelopes.
  
  
  RESULTS
  In this work we characterise the function of the Drosophila cold gene, that codes for a protein belonging to the Ly6 superfamily of extracellular ligands. Analysis of cold mutants shows that this gene is specifically required for the organisation of the septate junctions in epithelial tissues and in the nervous system, where its contribution is essential for the maintenance of the blood-brain barrier. We show that cold acts in a cell autonomous way, and we present evidence indicating that this protein could act as a septate junction component.
  
  
  CONCLUSIONS
  We discuss the specific roles of cold and three other Drosophila members of the Ly6 superfamily that have been shown to participate in a non-redundant way in the process of septate junction assembly. We propose that vertebrate Ly6 proteins could fulfill analogous roles in tight junctions and/or paranodal septate junctions.
authors.affiliation: Université de Toulouse, UPS, Centre de Biologie du Développement, Université Paul Sabatier, Toulouse, France.
authors.forename: Assia
authors.initials: A
authors.lastname: Hijazi
authors.forename: Marc
authors.initials: M
authors.lastname: Haenlin
authors.forename: Lucas
authors.initials: L
authors.lastname: Waltzer
authors.forename: Fernando
authors.initials: F
authors.lastname: Roch
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001812:Blood-Brain Barrier / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism; D029721:Drosophila Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D004331:Drosophila melanogaster / Q000166:cytology / Q000196:embryology / Q000378:metabolism*; D004475:Ectoderm / Q000166:cytology / Q000378:metabolism; D004625:Embryo, Nonmammalian / Q000166:cytology / Q000378:metabolism; D004847:Epithelial Cells / Q000166:cytology / Q000378:metabolism; D017344:Genes, Insect / Q000235:genetics; D007814:Larva / Q000166:cytology / Q000378:metabolism; D008969:Molecular Sequence Data; D009024:Morphogenesis; D009457:Neuroglia / Q000166:cytology / Q000378:metabolism; D010641:Phenotype; D021381:Protein Transport; D012469:Salivary Glands / Q000166:cytology / Q000378:metabolism; D013347:Subcellular Fractions / Q000378:metabolism; D019108:Tight Junctions / Q000378:metabolism*; D014132:Trachea / Q000166:cytology / Q000196:embryology / Q000378:metabolism; D014921:Wings, Animal / Q000166:cytology / Q000378:metabolism
chemical_list: D029721:Drosophila Proteins