Evidence map›Paper›PMID 38917328›Full record

ArticleNucleic acids research2024

SUMO protease and proteasome recruitment at the nuclear periphery differently affect replication dynamics at arrested forks.

Kamila Schirmeisen, Karel Naiman, Karine Fréon, Laetitia Besse, Shrena Chakraborty, Anissia Ait Saada, Antony M Carr, Karol Kramarz, Sarah A E Lambert

Abstract read
In one paragraph

Article in Nucleic acids research, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
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  7. Review
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  9. Review
  10. Article
  11. Article
  12. Multifaceted roles of SUMO in DNA metabolism.Nucleus (Austin, Tex.) · 2024
    Review
  13. Article
  14. Review
  15. Article
  16. Ubiquitin and SUMO pathways in DNA replication and replication-coupled repair.Critical reviews in biochemistry and molecular biology
    Review
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

9 authors.

Kamila SchirmeisenInstitut Curie, Université PSL, CNRS UMR3348, 91400 Orsay, France.
Karel NaimanINSERM U1068, CNRS UMR7258, Aix Marseille Univ U105, Institut Paoli-Calmettes, CRCM, Marseille, France.
Karine FréonInstitut Curie, Université PSL, CNRS UMR3348, 91400 Orsay, France.
Laetitia BesseInstitut Curie, Université PSL, CNRS UAR2016, Inserm US43, Université Paris-Saclay, Multimodal Imaging Center, 91400 Orsay, France.
Shrena ChakrabortyInstitut Curie, Université PSL, CNRS UMR3348, 91400 Orsay, France.
Anissia Ait SaadaInstitut Curie, Université PSL, CNRS UMR3348, 91400 Orsay, France.
Antony M CarrGenome Damage and Stability Centre, School of Life Sciences, University of Sussex, Falmer BN1 9RQ, UK.
Karol KramarzAcademic Excellence Hub - Research Centre for DNA Repair and Replication, Faculty of Biological Sciences, University of Wroclaw, 50-328 Wroclaw, Poland.
Sarah A E LambertInstitut Curie, Université PSL, CNRS UMR3348, 91400 Orsay, France.ORCID 0000-0002-1403-3204

Funding

Ames Research Center NASAANR ANR-23-CE12-0007-01CNRSExcellence Initiative - Research UniversityFondation LIGUE EL2020LNCC/SalInstitut CurieLIGUENIRO ANR-19-CE12-0023-01University of Wrocław IDN.CBNDR 0320/2020/20Wellcome 110047/Z/15/ZWellcome Trust
6 · The paper itself

Abstract

Nuclear pore complexes (NPCs) have emerged as genome organizers, defining a particular nuclear compartment enriched for SUMO protease and proteasome activities, and act as docking sites for the repair of DNA damage. In fission yeast, the anchorage of perturbed replication forks to NPCs is an integral part of the recombination-dependent replication restart mechanism (RDR) that resumes DNA synthesis at terminally dysfunctional forks. By mapping DNA polymerase usage, we report that SUMO protease Ulp1-associated NPCs ensure efficient initiation of restarted DNA synthesis, whereas proteasome-associated NPCs sustain the progression of restarted DNA polymerase. In contrast to Ulp1-dependent events, this last function is not alleviated by preventing SUMO chain formation. By analyzing the role of the nuclear basket, the nucleoplasmic extension of the NPC, we reveal that the activities of Ulp1 and the proteasome cannot compensate for each other and affect the dynamics of RDR in distinct ways. Our work probes two distinct mechanisms by which the NPC environment ensures optimal RDR, both controlled by different NPC components.

Indexed as

DNA ReplicationNuclear PoreProteasome Endopeptidase ComplexSchizosaccharomycesSchizosaccharomyces pombe ProteinsCell NucleusCysteine EndopeptidasesCysteine EndopeptidasesProteasome Endopeptidase ComplexSchizosaccharomyces pombe ProteinsUlp1 protease

Identifiers

PMID38917328
PMCPMC11317160

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Registered trials

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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.