title: p120-catenin-dependent junctional recruitment of Shroom3 is required for apical constriction during lens pit morphogenesis.
abstract: Apical constriction (AC) is a widely utilized mechanism of cell shape change whereby epithelial cells transform from a cylindrical to conical shape, which can facilitate morphogenetic movements during embryonic development. Invertebrate epithelial cells undergoing AC depend on the contraction of apical cortex-spanning actomyosin filaments that generate force on the apical junctions and pull them toward the middle of the cell, effectively reducing the apical circumference. A current challenge is to determine whether these mechanisms are conserved in vertebrates and to identify the molecules responsible for linking apical junctions with the AC machinery. Utilizing the developing mouse eye as a model, we have uncovered evidence that lens placode AC may be partially dependent on apically positioned myosin-containing filaments associated with the zonula adherens. In addition we found that, among several junctional components, p120-catenin genetically interacts with Shroom3, a protein required for AC during embryonic morphogenesis. Further analysis revealed that, similar to Shroom3, p120-catenin is required for AC of lens cells. Finally, we determined that p120-catenin functions by recruiting Shroom3 to adherens junctions. Together, these data identify a novel role for p120-catenin during AC and further define the mechanisms required for vertebrate AC.
authors.affiliation: The Visual System Group, Division of Pediatric Ophthalmology and Developmental Biology, Children's Hospital Research Foundation, University of Cincinnati, Cincinnati, OH 45229, USA.
authors.forename: Richard A
authors.initials: RA
authors.lastname: Lang
authors.affiliation: College of Optometry, The Ohio State University, Columbus, OH 43210, USA.
authors.forename: Ken
authors.initials: K
authors.lastname: Herman
authors.affiliation: Department of Cancer Biology, Vanderbilt University, Nashville, TN 37232, USA.
authors.forename: Albert B
authors.initials: AB
authors.lastname: Reynolds
authors.affiliation: Department of Biological Sciences, University of Pittsburgh, Pittsburgh, PA 15260, USA.
authors.forename: Jeffrey D
authors.initials: JD
authors.lastname: Hildebrand
authors.affiliation: College of Optometry, The Ohio State University, Columbus, OH 43210, USA plageman.3@osu.edu.
authors.forename: Timothy F
authors.initials: TF
authors.lastname: Plageman
mesh_terms: D000205:Actomyosin / Q000378:metabolism; D022005:Adherens Junctions / Q000378:metabolism; D000818:Animals; D051177:Catenins / Q000502:physiology*; D003599:Cytoskeleton / Q000378:metabolism; D017353:Gene Deletion; D018507:Gene Expression Regulation, Developmental; D005838:Genotype; D007908:Lens, Crystalline / Q000196:embryology*; D051379:Mice; D008822:Mice, Transgenic; D008840:Microfilament Proteins / Q000235:genetics / Q000502:physiology*; D009024:Morphogenesis; D024501:Nonmuscle Myosin Type IIB / Q000378:metabolism; D013997:Time Factors; D000095002:Delta Catenin
chemical_list: D051177:Catenins; D008840:Microfilament Proteins; C402112:Shrm protein, mouse; D000205:Actomyosin; D024501:Nonmuscle Myosin Type IIB; D000095002:Delta Catenin; C000722349:Ctnnd1 protein, mouse
keywords: Apical constriction; Invagination; Lens pit morphogenesis; Shroom3; delta1 catenin (Ctnnd1); p120-catenin