title: Posttranslational marks control architectural and functional plasticity of the nuclear pore complex basket.
abstract: The nuclear pore complex (NPC) serves as both the unique gate between the nucleus and the cytoplasm and a major platform that coordinates nucleocytoplasmic exchanges, gene expression, and genome integrity. To understand how the NPC integrates these functional constraints, we dissected here the posttranslational modifications of the nuclear basket protein Nup60 and analyzed how they intervene to control the plasticity of the NPC. Combined approaches highlight the role of monoubiquitylation in regulating the association dynamics of Nup60 and its partner, Nup2, with the NPC through an interaction with Nup84, a component of the Y complex. Although major nuclear transport routes are not regulated by Nup60 modifications, monoubiquitylation of Nup60 is stimulated upon genotoxic stress and regulates the DNA-damage response and telomere repair. Together, these data reveal an original mechanism contributing to the plasticity of the NPC at a molecular-organization and functional level.
authors.affiliation: University Paris Diderot, Sorbonne Paris Cité, Pathologie et Virologie Moléculaire, Institut National de la Santé et de la Recherche Medicale (INSERM), Centre National de la Recherche Scientifique (CNRS), Equipe labellisée Ligue contre le cancer, Hôpital St. Louis, 75475 Paris, France.
authors.forename: Carlos A
authors.initials: CA
authors.lastname: Niño
authors.affiliation: University Paris Diderot, Sorbonne Paris Cité, Pathologie et Virologie Moléculaire, Institut National de la Santé et de la Recherche Medicale (INSERM), Centre National de la Recherche Scientifique (CNRS), Equipe labellisée Ligue contre le cancer, Hôpital St. Louis, 75475 Paris, France.
authors.forename: David
authors.initials: D
authors.lastname: Guet
authors.affiliation: University Paris Diderot, Sorbonne Paris Cité, Pathologie et Virologie Moléculaire, Institut National de la Santé et de la Recherche Medicale (INSERM), Centre National de la Recherche Scientifique (CNRS), Equipe labellisée Ligue contre le cancer, Hôpital St. Louis, 75475 Paris, France.
authors.forename: Alexandre
authors.initials: A
authors.lastname: Gay
authors.affiliation: University Paris Diderot, Sorbonne Paris Cité, Pathologie et Virologie Moléculaire, Institut National de la Santé et de la Recherche Medicale (INSERM), Centre National de la Recherche Scientifique (CNRS), Equipe labellisée Ligue contre le cancer, Hôpital St. Louis, 75475 Paris, France.
authors.forename: Sergine
authors.initials: S
authors.lastname: Brutus
authors.affiliation: Aix-Marseille University, CNRS UMR 7258, INSERM UMR1068, Institut Paoli-Calmettes, Cancer Research Center of Marseille, Equipe labellisée Ligue contre le cancer, 13273 Marseille, France.
authors.forename: Frédéric
authors.initials: F
authors.lastname: Jourquin
authors.affiliation: University Paris Diderot, Sorbonne Paris Cité, Pathologie et Virologie Moléculaire, Institut National de la Santé et de la Recherche Medicale (INSERM), Centre National de la Recherche Scientifique (CNRS), Equipe labellisée Ligue contre le cancer, Hôpital St. Louis, 75475 Paris, France.
authors.forename: Shweta
authors.initials: S
authors.lastname: Mendiratta
authors.affiliation: Institut Curie, PSL Research University, CNRS UMR 144, Pierre-and-Marie-Curie Université, Team-Space time imaging of endomembranes and organelles dynamics and PICT-IBiSA Imaging Core Facility, 75005 Paris, France.
authors.forename: Jean
authors.initials: J
authors.lastname: Salamero
authors.affiliation: Aix-Marseille University, CNRS UMR 7258, INSERM UMR1068, Institut Paoli-Calmettes, Cancer Research Center of Marseille, Equipe labellisée Ligue contre le cancer, 13273 Marseille, France.
authors.forename: Vincent
authors.initials: V
authors.lastname: Géli
authors.affiliation: University Paris Diderot, Sorbonne Paris Cité, Pathologie et Virologie Moléculaire, Institut National de la Santé et de la Recherche Medicale (INSERM), Centre National de la Recherche Scientifique (CNRS), Equipe labellisée Ligue contre le cancer, Hôpital St. Louis, 75475 Paris, France catherine.dargemont@inserm.fr.
authors.forename: Catherine
authors.initials: C
authors.lastname: Dargemont
mesh_terms: D021581:Active Transport, Cell Nucleus; D003546:Cysteine Endopeptidases; D008239:Lysine / Q000378:metabolism; D008856:Microscopy, Fluorescence; D028861:Nuclear Pore Complex Proteins / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D012441:Saccharomyces cerevisiae / Q000378:metabolism* / Q000648:ultrastructure; D029701:Saccharomyces cerevisiae Proteins / Q000378:metabolism*; D014452:Ubiquitins / Q000378:metabolism
chemical_list: C097894:NUP84 protein, S cerevisiae; D028861:Nuclear Pore Complex Proteins; C495208:Nup60 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D014452:Ubiquitins; D003546:Cysteine Endopeptidases; C118083:Ulp1 protease; D008239:Lysine