Evidence map›Paper›PMID 17538013›Full record

ArticleMolecular biology of the cell2007

Nucleoporins prevent DNA damage accumulation by modulating Ulp1-dependent sumoylation processes.

Benoit Palancade, Xianpeng Liu, Maria Garcia-Rubio, Andrès Aguilera, Xiaolan Zhao, Valérie Doye

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 93 papers.

0numbers the graph read from it
0cells of the map it votes in
93citing papers in PubMed
3.1field-weighted citation impact, top 8% of its field
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

93 citing papers in PubMed, 141 citations in OpenAlex.

  1. Review
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  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. Multifaceted roles of SUMO in DNA metabolism.Nucleus (Austin, Tex.) · 2024
    Review
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  11. Review
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  13. Review
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33 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 3 institutions in 3 countries.

Benoit PalancadeInstitut Curie, Centre de Recherche, and Unité Mixte de Recherche 144 Centre National de la Recherche Scientifique, F-75248 Paris, France. palancad@crie.fr
Xianpeng Liu
Maria Garcia-Rubio
Andrès Aguilera
Xiaolan Zhao
Valérie Doye
Centre National de la Recherche Scientifique · FRConsejo Superior de Investigaciones Científicas · ESMemorial Sloan Kettering Cancer Center · US

Funding

The Rtt107 interactome structures and functionsR01GM080670 · NIGMS · SLOAN-KETTERING INST CAN RESEARCH · PI ZHAO, XIAOLAN · 2007 to 2021
$4.5M
6 · The paper itself

Abstract

Increasing evidences suggest that nuclear pore complexes (NPCs) control different aspects of nuclear metabolism, including transcription, nuclear organization, and DNA repair. We previously established that the Nup84 complex, a major NPC building block, is part of a genetic network involved in DNA repair. Here, we show that double-strand break (DSB) appearance is linked to a shared function of the Nup84 and the Nup60/Mlp1-2 complexes. Mutants within these complexes exhibit similar genetic interactions and alteration in DNA repair processes as mutants of the SUMO-protease Ulp1. Consistently, these nucleoporins are required for maintenance of proper Ulp1 levels at NPCs and for the establishment of the appropriate sumoylation of several cellular proteins, including the DNA repair factor Yku70. Moreover, restoration of nuclear envelope-associated Ulp1 in nucleoporin mutants reestablishes proper sumoylation patterns and suppresses DSB accumulation and genetic interactions with DNA repair genes. Our results thus provide a molecular mechanism that underlies the connection between NPC and genome stability.

Indexed as

DNA DamageCysteine EndopeptidasesDNA Breaks, Double-StrandedDNA RepairEnzyme StabilityKaryopherinsMutationNuclear EnvelopeNuclear Pore Complex ProteinsNuclear ProteinsPhenotypeProtein TransportRNA-Binding ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSmall Ubiquitin-Related Modifier ProteinsCysteine EndopeptidasesKaryopherinsMLP1 protein, S cerevisiaeNuclear Pore Complex ProteinsNuclear ProteinsRNA-Binding ProteinsSaccharomyces cerevisiae ProteinsSmall Ubiquitin-Related Modifier ProteinsUlp1 protease

Identifiers

PMID17538013
PMCPMC1949349
OpenAlexW2135144130

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.