title: Adhesion disengagement uncouples intrinsic and extrinsic forces to drive cytokinesis in epithelial tissues.
abstract: Cytokinesis entails cell invagination by a contractile actomyosin ring. In epithelia, E-cadherin-mediated adhesion connects the cortices of contacting cells; thus, it is unclear how invagination occurs, how the new junction forms, and how tissue integrity is preserved. Investigations in Drosophila embryos first show that apicobasal cleavage is polarized: invagination is faster from the basal than from the apical side. Ring contraction but not its polarized constriction is controlled by septin filaments and Anillin. Polarized cleavage is due instead to mechanical anchorage of the ring to E-cadherin complexes. Formation of the new junction requires local adhesion disengagement in the cleavage furrow, followed by new E-cadherin complex formation at the new interface. E-cadherin disengagement depends on the tension exerted by the cytokinetic ring and by neighboring cells. We uncover intrinsic and extrinsic forces necessary for cytokinesis and present a framework for understanding how tissue cohesion is preserved during epithelial division.
authors: Aix-Marseille Université, CNRS UMR 7288, IBDM, Campus de Luminy, Case 907, 13288 Marseille Cedex 09, France.
authors: Charlène
authors: C
authors: Guillot
authors: Thomas
authors: T
authors: Lecuit
mesh_terms: D000199:Actins / Q000235:genetics / Q000378:metabolism; D000205:Actomyosin / Q000378:metabolism; D000818:Animals; D015820:Cadherins / Q000235:genetics / Q000378:metabolism; D002448:Cell Adhesion / Q000235:genetics* / Q000502:physiology; D002455:Cell Division / Q000235:genetics; D016764:Cell Polarity / Q000235:genetics; D003285:Contractile Proteins / Q000378:metabolism; D048749:Cytokinesis / Q000235:genetics; D003599:Cytoskeleton / Q000378:metabolism; D004331:Drosophila melanogaster / Q000166:cytology / Q000196:embryology / Q000378:metabolism; D047108:Embryonic Development / Q000235:genetics; D004848:Epithelium / Q000254:growth & development / Q000378:metabolism; D058112:Septins / Q000235:genetics / Q000378:metabolism
chemical_list: D000199:Actins; D015820:Cadherins; D003285:Contractile Proteins; C095886:anillin; D000205:Actomyosin; D058112:Septins