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Suppression of epithelial folding at actomyosin-enriched compartment boundaries downstream of Wingless signalling

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Scarpa, E 


Epithelial folding shapes embryos and tissues during development. Here, we investigate the coupling between epithelial folding and actomyosin-enriched compartmental boundaries. The mechanistic relationship between the two is unclear, because actomyosin-enriched boundaries are not necessarily associated with folds. Also, some cases of epithelial folding occur independently of actomyosin contractility. We investigated the shallow folds called parasegment grooves that form at boundaries between anterior and posterior compartments in the early Drosophila embryo. We demonstrate that formation of these folds requires the presence of an actomyosin enrichment along the boundary cell-cell contacts. These enrichments, which require Wingless signalling, increase interfacial tension not only at the level of the adherens junctions but also along the lateral surfaces. We find that epithelial folding is normally under inhibitory control because different genetic manipulations, including depletion of the Myosin II phosphatase Flapwing, increase the depth of folds at boundaries. Fold depth correlates with the levels of Bazooka (Baz), the Par-3 homologue, along the boundary cell-cell contacts. Moreover, Wingless and Hedgehog signalling have opposite effects on fold depth at the boundary that correlate with changes in Baz planar polarity.



Apico-basal polarity, Contractility, Embryo, Epithelium, Morphogenesis, Planar polarity, Actomyosin, Adherens Junctions, Animals, Animals, Genetically Modified, Bacterial Proteins, Body Patterning, Drosophila Proteins, Drosophila melanogaster, Epithelium, Gene Knockdown Techniques, Genes, Insect, Green Fluorescent Proteins, Hedgehog Proteins, Intracellular Signaling Peptides and Proteins, Luminescent Proteins, Mutation, Myosin Type II, Myosin-Light-Chain Phosphatase, Signal Transduction, Wnt1 Protein

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The Company of Biologists
Wellcome Trust (099234/Z/12/Z)
Engineering and Physical Sciences Research Council (EP/R025398/1)
Biotechnology and Biological Sciences Research Council (BB/J010278/1)
Wellcome Trust (099130/Z/12/Z)
Wellcome Trust (207553/Z/17/Z)
This work was supported by the Biotechnology and Biological Sciences Research Council (BBSRC) [BB/J010278/1] and the Wellcome Trust [099234/Z/12/Z to B.S.; 099130/Z/12/Z to CAIC]. J.M.U. was supported by a Postdoctoral Fellowship [I-D+i 2008-2011] from Ministerio de Educación, Cultura y Deporte (Spanish Ministry of Education), E.S. by a University of Cambridge Herchel Smith Postdoctoral Fellowship and L.M. by an Engineering and Physical Sciences Research Council (EPSRC) Research Software Engineer Fellowship. Deposited in PMC for immediate release.
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