title: C. elegans Anillin proteins regulate intercellular bridge stability and germline syncytial organization.
abstract: Cytokinesis generally produces two separate daughter cells, but in some tissues daughter nuclei remain connected to a shared cytoplasm, or syncytium, through incomplete cytokinesis. How syncytia form remains poorly understood. We studied syncytial formation in the Caenorhabditis elegans germline, in which germ cells connect to a shared cytoplasm core (the rachis) via intercellular bridges. We found that syncytial architecture initiates early in larval development, and germ cells become progressively interconnected until adulthood. The short Anillin family scaffold protein ANI-2 is enriched at intercellular bridges from the onset of germ cell specification, and ANI-2 loss resulted in destabilization of intercellular bridges and germ cell multinucleation defects. These defects were partially rescued by depleting the canonical Anillin ANI-1 or blocking cytoplasmic streaming. ANI-2 is also required for elastic deformation of the gonad during ovulation. We propose that ANI-2 promotes germ cell syncytial organization and allows for compensation of the mechanical stress associated with oogenesis by conferring stability and elasticity to germ cell intercellular bridges.
authors: Institute of Research in Immunology and Cancer and Department of Pathology and Cell Biology, Université de Montréal, Montréal, Québec H3C 3J7, Canada.
authors: Rana
authors: R
authors: Amini
authors: Institute of Research in Immunology and Cancer and Department of Pathology and Cell Biology, Université de Montréal, Montréal, Québec H3C 3J7, Canada.
authors: Eugénie
authors: E
authors: Goupil
authors: Department of Biology, McGill University, Montréal, Québec H2A 1B1, Canada.
authors: Sara
authors: S
authors: Labella
authors: Department of Biology, McGill University, Montréal, Québec H2A 1B1, Canada.
authors: Monique
authors: M
authors: Zetka
authors: Institute of Research in Immunology and Cancer and Department of Pathology and Cell Biology, Université de Montréal, Montréal, Québec H3C 3J7, CanadaInstitute of Research in Immunology and Cancer and Department of Pathology and Cell Biology, Université de Montréal, Montréal, Québec H3C 3J7, Canada.
authors: Amy S
authors: AS
authors: Maddox
authors: Institute of Research in Immunology and Cancer and Department of Pathology and Cell Biology, Université de Montréal, Montréal, Québec H3C 3J7, CanadaInstitute of Research in Immunology and Cancer and Department of Pathology and Cell Biology, Université de Montréal, Montréal, Québec H3C 3J7, Canada chartier.nico@gmail.com jc.labbe@umontreal.ca.
authors: Jean-Claude
authors: JC
authors: Labbé
authors: Institute of Research in Immunology and Cancer and Department of Pathology and Cell Biology, Université de Montréal, Montréal, Québec H3C 3J7, Canada chartier.nico@gmail.com jc.labbe@umontreal.ca.
authors: Nicolas T
authors: NT
authors: Chartier
mesh_terms: D000818:Animals; D017173:Caenorhabditis elegans / Q000166:cytology / Q000378:metabolism*; D029742:Caenorhabditis elegans Proteins / Q000502:physiology*; D003595:Cytoplasmic Streaming; D005260:Female; D005854:Germ Cells / Q000378:metabolism; D015726:Giant Cells / Q000502:physiology*; D006066:Gonads / Q000166:cytology; D007365:Intercellular Junctions / Q000378:metabolism*; D007814:Larva / Q000166:cytology / Q000378:metabolism; D008297:Male; D008840:Microfilament Proteins / Q000502:physiology*; D009866:Oogenesis; D055550:Protein Stability
chemical_list: C502567:ANI-2 protein, C elegans; D029742:Caenorhabditis elegans Proteins; D008840:Microfilament Proteins