Evidence map›Paper›PMID 32402281›Full record

ArticleCell reports2020

Relocation of Collapsed Forks to the Nuclear Pore Complex Depends on Sumoylation of DNA Repair Proteins and Permits Rad51 Association.

Jenna M Whalen, Nalini Dhingra, Lei Wei, Xiaolan Zhao, Catherine H Freudenreich

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
3.5field-weighted citation impact, top 6% 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

54 citing papers in PubMed, 71 citations in OpenAlex.

  1. Review
  2. The Role of Arp2/3 in End-Resection During DNA Double-Strand Break Repair.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026
    Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. 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
  16. Article
  17. Multifaceted roles of SUMO in DNA metabolism.Nucleus (Austin, Tex.) · 2024
    Review
  18. Article
  19. Article
  20. Article
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

5 authors at 2 institutions in 1 country.

Jenna M WhalenDepartment of Biology, Tufts University, Medford, MA 02155, USA.
Nalini DhingraMolecular Biology Program, Memorial Sloan Kettering Cancer Center, New York, NY 10065, USA.
Lei WeiMolecular Biology Program, Memorial Sloan Kettering Cancer Center, New York, NY 10065, USA.
Xiaolan ZhaoMolecular Biology Program, Memorial Sloan Kettering Cancer Center, New York, NY 10065, USA.
Catherine H FreudenreichDepartment of Biology, Tufts University, Medford, MA 02155, USA; Program in Genetics, Tufts University, Boston, MA 02111, USA. Electronic address: catherine.freudenreich@tufts.edu.
Memorial Sloan Kettering Cancer Center · USTufts University · US

Funding

X-RAY CRYSTALLOGRAPHYP30CA008748 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI Hongbiao Carl Lekaye · 1985 to 2026
$347.4M
The Rtt107 interactome structures and functionsR01GM080670 · NIGMS · SLOAN-KETTERING INST CAN RESEARCH · PI ZHAO, XIAOLAN · 2007 to 2021
$4.5M
Regulation of Replication and Recombination IntermediatesR01GM131058 · NIGMS · SLOAN-KETTERING INST CAN RESEARCH · PI ZHAO, XIAOLAN · 2019 to 2022
$1.6M
Fork Restart at Replication Barriers and Effects on Genome StabilityR01GM122880 · NIGMS · TUFTS UNIVERSITY MEDFORD · PI FREUDENREICH, CATHERINE H · 2017 to 2020
$1.4M
NCI NIH HHS P30 CA008748NIGMS NIH HHS R01 GM080670NIGMS NIH HHS R01 GM122880NIGMS NIH HHS R01 GM131058
6 · The paper itself

Abstract

Expanded CAG repeats form stem-loop secondary structures that lead to fork stalling and collapse. Previous work has shown that these collapsed forks relocalize to nuclear pore complexes (NPCs) in late S phase in a manner dependent on replication, the nucleoporin Nup84, and the Slx5 protein, which prevents repeat fragility and instability. Here, we show that binding of the Smc5/6 complex to the collapsed fork triggers Mms21-dependent sumoylation of fork-associated DNA repair proteins, and that RPA, Rad52, and Rad59 are the key sumoylation targets that mediate relocation. The SUMO interacting motifs of Slx5 target collapsed forks to the NPC. Notably, Rad51 foci only co-localize with the repeat after it is anchored to the nuclear periphery and Rad51 exclusion from the early collapsed fork is dependent on RPA sumoylation. This pathway may provide a mechanism to constrain recombination at stalled or collapsed forks until it is required for fork restart.

Indexed as

DNA RepairDNA ReplicationCell Cycle ProteinsNuclear PoreRad51 RecombinaseRecombination, GeneticSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSUMO-1 ProteinSumoylationCell Cycle ProteinsMms21 protein, S cerevisiaeRAD51 protein, S cerevisiaeRad51 RecombinaseSaccharomyces cerevisiae ProteinsSMC5 protein, S cerevisiaeSMC6 protein, S cerevisiaeSUMO-1 ProteinCAG repeatfork collapsefork relocationnuclear pore complexRad52 Rad59 sumoylationreplication forkRPA sumoylationSmc5-Smc6trinucleotide repeat

Identifiers

PMID32402281
PMCPMC7344339
OpenAlexW3025080788

What OpenQuestion holds

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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.