Evidence map›Paper›PMID 26051542›Full record

ArticleDevelopmental cell2015

Nup153 Recruits the Nup107-160 Complex to the Inner Nuclear Membrane for Interphasic Nuclear Pore Complex Assembly.

Benjamin Vollmer, Michael Lorenz, Daniel Moreno-Andrés, Mona Bodenhöfer, Paola De Magistris, Susanne Adina Astrinidis, Allana Schooley, Matthias Flötenmeyer, Sebastian Leptihn, Wolfram Antonin

Abstract read
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In one paragraph

Article in Developmental cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 papers.

0numbers the graph read from it
0cells of the map it votes in
85citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

85 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Structure, function and assembly of nuclear pore complexes.Nature reviews. Molecular cell biology · 2026
    Review
  7. Article
  8. Nucleoporins cooperate with Polycomb silencers to promote transcriptional repression and repair at DNA double-strand breaks.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  9. Article
  10. Article
  11. Article
  12. Liposome Floatation Assays to Study Membrane Interactions of Nucleoporins.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. The Molecular Architecture of the Nuclear Basket.bioRxiv : the preprint server for biology · 2024
    Article
  20. Review

25 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors.

Benjamin VollmerFriedrich Miescher Laboratory of the Max Planck Society, Spemannstraße 39, 72076 Tübingen, Germany.
Michael LorenzFriedrich Miescher Laboratory of the Max Planck Society, Spemannstraße 39, 72076 Tübingen, Germany.
Daniel Moreno-AndrésFriedrich Miescher Laboratory of the Max Planck Society, Spemannstraße 39, 72076 Tübingen, Germany.
Mona BodenhöferFriedrich Miescher Laboratory of the Max Planck Society, Spemannstraße 39, 72076 Tübingen, Germany.
Paola De MagistrisFriedrich Miescher Laboratory of the Max Planck Society, Spemannstraße 39, 72076 Tübingen, Germany.
Susanne Adina AstrinidisFriedrich Miescher Laboratory of the Max Planck Society, Spemannstraße 39, 72076 Tübingen, Germany.
Allana SchooleyFriedrich Miescher Laboratory of the Max Planck Society, Spemannstraße 39, 72076 Tübingen, Germany.
Matthias FlötenmeyerMax Planck Institute for Developmental Biology, Spemannstraße 37, 72076 Tübingen, Germany.
Sebastian LeptihnInstitute for Microbiology and Molecular Biology, University of Hohenheim, Garbenstraße 30, 70599 Stuttgart, Germany.
Wolfram AntoninFriedrich Miescher Laboratory of the Max Planck Society, Spemannstraße 39, 72076 Tübingen, Germany. Electronic address: wolfram.antonin@tuebingen.mpg.de.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In metazoa, nuclear pore complexes (NPCs) are assembled from constituent nucleoporins by two distinct mechanisms: in the re-forming nuclear envelope at the end of mitosis and into the intact nuclear envelope during interphase. Here, we show that the nucleoporin Nup153 is required for NPC assembly during interphase but not during mitotic exit. It functions in interphasic NPC formation by binding directly to the inner nuclear membrane via an N-terminal amphipathic helix. This binding facilitates the recruitment of the Nup107-160 complex, a crucial structural component of the NPC, to assembly sites. Our work further suggests that the nuclear transport receptor transportin and the small GTPase Ran regulate the interaction of Nup153 with the membrane and, in this way, direct pore complex assembly to the nuclear envelope during interphase.

Indexed as

Active Transport, Cell NucleusAmino Acid SequenceAnimalsHeLa CellsHumansInterphaseKaryopherinsModels, BiologicalMolecular Sequence DataMutagenesis, Site-DirectedNuclear EnvelopeNuclear PoreNuclear Pore Complex ProteinsNuclear ProteinsProtein Interaction Domains and Motifsran GTP-Binding ProteinKaryopherinsNuclear Pore Complex ProteinsNuclear ProteinsNUP107 protein, humanNUP153 protein, humanNup153 protein, XenopusNUP160 protein, humanNup160 protein, Xenopusran GTP-Binding ProteinRecombinant ProteinsXenopus Proteins

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.