Drosophila morphogenesis: Orchestrating cell rearrangements

AbstractChanges in shape of individual cells need to be coordinated to generate the movements of cell groups and sheets that are so important in morphogenesis. Recent results have shown that, during Drosophila gastrulation, multiple signalling pathways act to orchestrate the complex cell rearrangements

bloated tubules (blot) Encodes a Drosophila Member of the Neurotransmitter Transporter Family Required for Organisation of the Apical Cytocortex

AbstractWe have identified a novel member of the vertebrate sodium- and chloride-dependent neurotransmitter symporter family from Drosophila melanogaster. This gene, named bloated tubules (blot), shows significant sequence similarity to a subgroup of vertebrate orphan transporters. blot transcripts are maternally supplied and during embryogenesis exhibit a complex and dynamic pattern in a subset of ectodermally derived epithelia, notably in the Malpighian tubules, and in the nervous system. Animals mutant for this gene are larval lethals, in which the Malpighian tubule cells are distended with an enlarged and disorganised apical surface. Embryos lacking the maternal component of blot expression die during early stages of development. They show an inability to form actin filaments in the apical cortex, resulting in impaired syncytial nuclear divisions, severe defects in the organisation of the cortical cytoskeleton, and a failure to cellularise. For the first time, a neurotransmitter transporter-like protein has been implicated in a function outside the nervous system. The isolation of blot thus provides the basis for an analysis of the relationship between the function of this putative transporter and epithelial morphogenesis

On the role of the MAGUK proteins encoded by Drosophila varicose during embryonic and postembryonic development

<p>Abstract</p> <p>Background</p> <p>Membrane-associated guanylate kinases (MAGUKs) form a family of scaffolding proteins, which are often associated with cellular junctions, such as the vertebrate tight junction, the <it>Drosophila </it>septate junction or the neuromuscular junction. Their capacity to serve as platforms for organising larger protein assemblies results from the presence of several protein-protein interaction domains. They often appear in different variants suggesting that they also mediate dynamic changes in the composition of the complexes.</p> <p>Results</p> <p>Here we show by electron microscopic analysis that <it>Drosophila </it>embryos lacking <it>varicose </it>function fail to develop septate junctions in the tracheae and the epidermis. In the embryo and in imaginal discs <it>varicose </it>expresses two protein isoforms, which belong to the MAGUK family. The two isoforms can be distinguished by the presence or absence of two L27 domains and are differentially affected in different <it>varicose </it>alleles. While the short isoform is essential for viability, the long isoform seems to have a supportive function. Varicose proteins co-localise with Neurexin IV in pleated septate junctions and are necessary, but not sufficient for its recruitment. The two proteins interact in vitro by the PDZ domain of Varicose and the four C-terminal amino acids of Neurexin IV. Postembryonic reduction of <it>varicose </it>function by expressing double-stranded RNA affects pattern formation and morphogenesis of the wing and the development of normal-shaped and -sized eyes.</p> <p>Conclusion</p> <p>Expression of two Varicose isoforms in embryonic epithelia and imaginal discs suggests that the composition of Varicose-mediated protein scaffolds at septate junctions is dynamic, which may have important implications for the modulation of their function.</p

Targeting of Drosophila Rhodopsin Requires Helix 8 but Not the Distal C-Terminus

BACKGROUND: The fundamental role of the light receptor rhodopsin in visual function and photoreceptor cell development has been widely studied. Proper trafficking of rhodopsin to the photoreceptor membrane is of great importance. In human, mutations in rhodopsin involving its intracellular mislocalization, are the most frequent cause of autosomal dominant Retinitis Pigmentosa, a degenerative retinal pathology characterized by progressive blindness. Drosophila is widely used as an animal model in visual and retinal degeneration research. So far, little is known about the requirements for proper rhodopsin targeting in Drosophila. METHODOLOGY/PRINCIPAL FINDINGS: Different truncated fly-rhodopsin Rh1 variants were expressed in the eyes of Drosophila and their localization was analyzed in vivo or by immunofluorescence. A mutant lacking the last 23 amino acids was found to properly localize in the rhabdomeres, the light-sensing organelle of the photoreceptor cells. This constitutes a major difference to trafficking in vertebrates, which involves a conserved QVxPA motif at the very C-terminus. Further truncations of Rh1 indicated that proper localization requires the last amino acid residues of a region called helix 8 following directly the last transmembrane domain. Interestingly, the very C-terminus of invertebrate visual rhodopsins is extremely variable but helix 8 shows conserved amino acid residues that are not conserved in vertebrate homologs. CONCLUSIONS/SIGNIFICANCE: Despite impressive similarities in the folding and photoactivation of vertebrate and invertebrate visual rhodopsins, a striking difference exists between mammalian and fly rhodopsins in their requirements for proper targeting. Most importantly, the distal part of helix 8 plays a central role in invertebrates. Since the last amino acid residues of helix 8 are dispensable for rhodopsin folding and function, we propose that this domain participates in the recognition of targeting factors involved in transport to the rhabdomeres

The apical protein Apnoia interacts with Crumbs to regulate tracheal growth and inflation

Most organs of multicellular organisms are built from epithelial tubes. To exert their functions, tubes rely on apico-basal polarity, on junctions, which form a barrier to separate the inside from the outside, and on a proper lumen, required for gas or liquid transport. Here we identify apnoia (apn), a novel Drosophila gene required for tracheal tube elongation and lumen stability at larval stages. Larvae lacking Apn show abnormal tracheal inflation and twisted airway tubes, but no obvious defects in early steps of tracheal maturation. apn encodes a transmembrane protein, primarily expressed in the tracheae, which exerts its function by controlling the localization of Crumbs (Crb), an evolutionarily conserved apical determinant. Apn physically interacts with Crb to control its localization and maintenance at the apical membrane of developing airways. In apn mutant tracheal cells, Crb fails to localize apically and is trapped in retromer-positive vesicles. Consistent with the role of Crb in apical membrane growth, RNAi-mediated knockdown of Crb results in decreased apical surface growth of tracheal cells and impaired axial elongation of the dorsal trunk. We conclude that Apn is a novel regulator of tracheal tube expansion in larval tracheae, the function of which is mediated by Crb