An evolutionarily conserved NPC subcomplex, which redistributes in part to kinetochores in mammalian cells

Author:

Belgareh Naïma1,Rabut Gwénaël2,Baï Siau Wei1,van Overbeek Megan1,Beaudouin Joël2,Daigle Nathalie2,Zatsepina Olga V.3,Pasteau Fabien1,Labas Valérie4,Fromont-Racine Micheline5,Ellenberg Jan2,Doye Valérie1

Affiliation:

1. UMR 144 Centre National de la Recherche Scientifique-Institut Curie, 75005 Paris, France

2. Gene Expression and Cell Biology/Biophysics Programmes, European Molecular Biology Laboratory, 69117 Heidelberg, Germany

3. UMR 218 Centre National de la Recherche Scientifique-Institut Curie, 75005 Paris, France

4. École Supérieure de Physique et de Chimie Industrielles-Centre National de la Recherche Scientifique, UMR 7637, 75005 Paris, France

5. Département des Biotechnologies, Institut Pasteur, 75015 Paris, France

Abstract

The nuclear pore complexes (NPCs) are evolutionarily conserved assemblies that allow traffic between the cytoplasm and the nucleus. In this study, we have identified and characterized a novel human nuclear pore protein, hNup133, through its homology with the Saccharomyces cerevisiae nucleoporin scNup133. Two-hybrid screens and immunoprecipitation experiments revealed a direct and evolutionarily conserved interaction between Nup133 and Nup84/Nup107 and indicated that hNup133 and hNup107 are part of a NPC subcomplex that contains two other nucleoporins (the previously characterized hNup96 and a novel nucleoporin designated as hNup120) homologous to constituents of the scNup84 subcomplex. We further demonstrate that hNup133 and hNup107 are localized on both sides of the NPC to which they are stably associated at interphase, remain associated as part of a NPC subcomplex during mitosis, and are targeted at early stages to the reforming nuclear envelope. Throughout mitosis, a fraction of hNup133 and hNup107 localizes to the kinetochores, thus revealing an unexpected connection between structural NPCs constituents and kinetochores. Photobleaching experiments further showed that the mitotic cytoplasm contains kinetochore-binding competent hNup133 molecules and that in contrast to its stable association with the NPCs the interaction of this nucleoporin with kinetochores is dynamic.

Publisher

Rockefeller University Press

Subject

Cell Biology

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