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

doi:10.1083/jcb.200101081

Published 17 September 2001. doi:10.1083/jcb.200101081

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© The Rockefeller University Press, 0021-9525/2001/9/1147 $5.00
The Journal of Cell Biology, Volume 154, Number 6, September 17, 2001 1147-1160

Article

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

Naïma Belgareh¹, Gwénaël Rabut², Siau Wei Baï¹, Megan van Overbeek¹, Joël Beaudouin², Nathalie Daigle², Olga V. Zatsepina³, Fabien Pasteau¹, Valérie Labas⁴, Micheline Fromont-Racine⁵, Jan Ellenberg² and Valérie Doye¹

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

Address correspondence to Valerie Doye, UMR 144 CNRS-Institut Curie, Section Recherche, 26 rue d'Ulm, 75248 Paris cedex 05, France. Tel.: 33-1-42-34-64-10. Fax: 33-1-42-34-64-21. E-mail: vdoye{at}curie.fr

The nuclear pore complexes (NPCs) are evolutionarily conservedassemblies that allow traffic between the cytoplasm and thenucleus. In this study, we have identified and characterizeda novel human nuclear pore protein, hNup133, through its homologywith the Saccharomyces cerevisiae nucleoporin scNup133. Two-hybridscreens and immunoprecipitation experiments revealed a directand evolutionarily conserved interaction between Nup133 andNup84/Nup107 and indicated that hNup133 and hNup107 are partof a NPC subcomplex that contains two other nucleoporins (thepreviously characterized hNup96 and a novel nucleoporin designatedas hNup120) homologous to constituents of the scNup84 subcomplex.We further demonstrate that hNup133 and hNup107 are localizedon both sides of the NPC to which they are stably associatedat interphase, remain associated as part of a NPC subcomplexduring mitosis, and are targeted at early stages to the reformingnuclear envelope. Throughout mitosis, a fraction of hNup133and hNup107 localizes to the kinetochores, thus revealing anunexpected connection between structural NPCs constituents andkinetochores. Photobleaching experiments further showed thatthe mitotic cytoplasm contains kinetochore-binding competenthNup133 molecules and that in contrast to its stable associationwith the NPCs the interaction of this nucleoporin with kinetochoresis dynamic.

Key Words: nucleoporin; nuclear pore; mitosis; kinetochores; GFP

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