title: Nucleocytoplasmic transport in the midzone membrane domain controls yeast mitotic spindle disassembly.
abstract: During each cell cycle, the mitotic spindle is efficiently assembled to achieve chromosome segregation and then rapidly disassembled as cells enter cytokinesis. Although much has been learned about assembly, how spindles disassemble at the end of mitosis remains unclear. Here we demonstrate that nucleocytoplasmic transport at the membrane domain surrounding the mitotic spindle midzone, here named the midzone membrane domain (MMD), is essential for spindle disassembly in Schizosaccharomyces pombe cells. We show that, during anaphase B, Imp1-mediated transport of the AAA-ATPase Cdc48 protein at the MMD allows this disassembly factor to localize at the spindle midzone, thereby promoting spindle midzone dissolution. Our findings illustrate how a separate membrane compartment supports spindle disassembly in the closed mitosis of fission yeast.
authors.affiliation: Centro Andaluz de Biología del Desarrollo. Universidad Pablo de Olavide/Consejo Superior de Investigaciones Cientificas, 41013 Sevilla, Spain Department of Molecular, Cell, and Developmental Biology, University of California, Santa Cruz, Santa Cruz, CA 95064.
authors.forename: Rafael
authors.initials: R
authors.lastname: Lucena
authors.affiliation: Department of Cell Biology, Harvard Medical School, Boston, MA 02115.
authors.forename: Noah
authors.initials: N
authors.lastname: Dephoure
authors.affiliation: Department of Cell Biology, Harvard Medical School, Boston, MA 02115.
authors.forename: Steve P
authors.initials: SP
authors.lastname: Gygi
authors.affiliation: Department of Molecular, Cell, and Developmental Biology, University of California, Santa Cruz, Santa Cruz, CA 95064.
authors.forename: Douglas R
authors.initials: DR
authors.lastname: Kellogg
authors.affiliation: Centro Andaluz de Biología del Desarrollo. Universidad Pablo de Olavide/Consejo Superior de Investigaciones Cientificas, 41013 Sevilla, Spain.
authors.forename: Victor A
authors.initials: VA
authors.lastname: Tallada
authors.affiliation: Centro Andaluz de Biología del Desarrollo. Universidad Pablo de Olavide/Consejo Superior de Investigaciones Cientificas, 41013 Sevilla, Spain rroddag@upo.es jjimmar@upo.es.
authors.forename: Rafael R
authors.initials: RR
authors.lastname: Daga
authors.affiliation: Centro Andaluz de Biología del Desarrollo. Universidad Pablo de Olavide/Consejo Superior de Investigaciones Cientificas, 41013 Sevilla, Spain rroddag@upo.es jjimmar@upo.es.
authors.forename: Juan
authors.initials: J
authors.lastname: Jimenez
mesh_terms: D021581:Active Transport, Cell Nucleus / Q000502:physiology; D000251:Adenosine Triphosphatases / Q000235:genetics / Q000378:metabolism; D000705:Anaphase / Q000502:physiology*; D018797:Cell Cycle Proteins / Q000235:genetics / Q000378:metabolism; D002467:Cell Nucleus / Q000235:genetics / Q000378:metabolism*; D012568:Schizosaccharomyces / Q000166:cytology / Q000235:genetics / Q000378:metabolism*; D029702:Schizosaccharomyces pombe Proteins / Q000235:genetics / Q000378:metabolism; D008941:Spindle Apparatus / Q000235:genetics / Q000378:metabolism*; D000074405:Valosin Containing Protein
chemical_list: D018797:Cell Cycle Proteins; D029702:Schizosaccharomyces pombe Proteins; D000251:Adenosine Triphosphatases; D000074405:Valosin Containing Protein