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Research Article
Mitotic checkpoint protein Mad1 is required for early Nup153 recruitment to chromatin and nuclear envelope integrity
Ikram Mossaid, Guillaume Chatel, Valérie Martinelli, Marcela Vaz, Birthe Fahrenkrog
Journal of Cell Science 2020 133: jcs249243 doi: 10.1242/jcs.249243 Published 3 November 2020
Ikram Mossaid
Institute of Molecular Biology and Medicine, Laboratory Biologie du Noyau, Université Libre de Bruxelles, 6041 Charleroi, Belgium
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Guillaume Chatel
Institute of Molecular Biology and Medicine, Laboratory Biologie du Noyau, Université Libre de Bruxelles, 6041 Charleroi, Belgium
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Valérie Martinelli
Institute of Molecular Biology and Medicine, Laboratory Biologie du Noyau, Université Libre de Bruxelles, 6041 Charleroi, Belgium
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Marcela Vaz
Institute of Molecular Biology and Medicine, Laboratory Biologie du Noyau, Université Libre de Bruxelles, 6041 Charleroi, Belgium
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Birthe Fahrenkrog
Institute of Molecular Biology and Medicine, Laboratory Biologie du Noyau, Université Libre de Bruxelles, 6041 Charleroi, Belgium
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  • ORCID record for Birthe Fahrenkrog
  • For correspondence: birthe.fahrenkrog@unibas.ch

Handling Editor: Maria Carmo-Fonseca

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ABSTRACT

Nucleoporin Nup153 is a multifunctional protein and a known binding partner of mitotic checkpoint protein Mad1 (also known as MAD1L1). The functional relevance of their interaction has remained elusive. Here, we have further dissected the interface and functional interplay of Nup153 and Mad1. Using in situ proximity ligation assays, we found that the presence of a nuclear envelope (NE) is a prerequisite for the Nup153–Mad1 association. Time-lapse microscopy revealed that depletion of Mad1 delayed recruitment of Nup153 to anaphase chromatin, which was often accompanied by a prolongation of anaphase. Furthermore, as seen by electron microscopic and three-dimensional structured illumination investigations, Nup153 and Mad1 depletion led to alterations in NE architecture, characterised by a change of membrane curvature at nuclear pore complexes (NPCs) and an expansion of the spacing between inner and outer nuclear membranes. Nup153 depletion, but not Mad1 depletion, caused defects in interphase NPC assembly, with partial displacement of cytoplasmic nucleoporins and a reduction in NPC density. Taken together, our results suggest that Nup153 has separable roles in NE and NPC formation: in post-mitotic NE re-formation in concert with Mad1 and in interphase NPC assembly, independent of Mad1.

Footnotes

  • Competing interests

    The authors declare no competing or financial interests.

  • Author contributions

    Conceptualization: I.M., G.C., V.M., B.F.; Validation: I.M., G.C., B.F.; Formal analysis: I.M., G.C., M.V., B.F.; Investigation: I.M., G.C., V.M., M.V.; Writing - original draft: I.M., B.F.; Writing - review & editing: G.C., B.F.; Supervision: B.F.; Project administration: B.F.; Funding acquisition: B.F.

  • Funding

    This work was supported by a FRIA PhD fellowship to I.M. and research grants to B.F. (grant numbers F.6006.10 and T.0237.13) from the Fonds De La Recherche Scientifique – FNRS.

  • Supplementary information

    Supplementary information available online at https://jcs.biologists.org/lookup/doi/10.1242/jcs.249243.supplemental

  • Received May 21, 2020.
  • Accepted September 24, 2020.
  • © 2020. Published by The Company of Biologists Ltd
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Keywords

  • Nuclear pore complex assembly
  • Mitotic checkpoint
  • Nup153
  • Mad1

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Research Article
Mitotic checkpoint protein Mad1 is required for early Nup153 recruitment to chromatin and nuclear envelope integrity
Ikram Mossaid, Guillaume Chatel, Valérie Martinelli, Marcela Vaz, Birthe Fahrenkrog
Journal of Cell Science 2020 133: jcs249243 doi: 10.1242/jcs.249243 Published 3 November 2020
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Research Article
Mitotic checkpoint protein Mad1 is required for early Nup153 recruitment to chromatin and nuclear envelope integrity
Ikram Mossaid, Guillaume Chatel, Valérie Martinelli, Marcela Vaz, Birthe Fahrenkrog
Journal of Cell Science 2020 133: jcs249243 doi: 10.1242/jcs.249243 Published 3 November 2020

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