Evidence map›Paper›PMID 25569253›Full record

ArticlePLoS genetics2015

Sumoylation influences DNA break repair partly by increasing the solubility of a conserved end resection protein.

Prabha Sarangi, Roland Steinacher, Veronika Altmannova, Qiong Fu, Tanya T Paull, Lumir Krejci, Matthew C Whitby, Xiaolan Zhao

Open access · goldAbstract read
In one paragraph

Article in PLoS genetics, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

27 citing papers in PubMed, 31 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Advances in SUMO-based regulation of homologous recombination.Current opinion in genetics & development · 2021
    Review
  5. Article
  6. ATM controls the extent of DNA end resection by eliciting sequential posttranslational modifications of CtIP.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. Roles of SUMO in Replication Initiation, Progression, and Termination.Advances in experimental medicine and biology · 2017
    Review
  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

8 authors at 4 institutions in 3 countries.

Prabha SarangiMolecular Biology Program, Memorial Sloan-Kettering Cancer Center, New York, New York, United States of America; Programs in Biochemistry, Cell, and Molecular Biology, Weill Cornell Graduate School of Medical Sciences, New York, New York, United States of America.
Roland SteinacherDepartment of Biochemistry, University of Oxford, Oxford, United Kingdom.
Veronika AltmannovaDepartment of Biology, Masaryk University, Brno, Czech Republic.
Qiong FuHoward Hughes Medical Institute, Department of Molecular Biosciences, and Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, Texas, United States of America.
Tanya T PaullHoward Hughes Medical Institute, Department of Molecular Biosciences, and Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, Texas, United States of America.
Lumir KrejciDepartment of Biology, Masaryk University, Brno, Czech Republic; National Centre for Biomolecular Research, Masaryk University, Brno, Czech Republic; International Clinical Research Center, St. Anne's University Hospital in Brno, Brno, Czech Republic.
Matthew C WhitbyDepartment of Biochemistry, University of Oxford, Oxford, United Kingdom.
Xiaolan ZhaoMolecular Biology Program, Memorial Sloan-Kettering Cancer Center, New York, New York, United States of America; Programs in Biochemistry, Cell, and Molecular Biology, Weill Cornell Graduate School of Medical Sciences, New York, New York, United States of America.
Howard Hughes Medical Institute · USMasaryk University · CZMemorial Sloan Kettering Cancer Center · USUniversity of Oxford · GB

Funding

X-RAY CRYSTALLOGRAPHYP30CA008748 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI Nicholas D Socci · 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
NCI NIH HHS P30 CA008748NIGMS NIH HHS GM080670NIGMS NIH HHS R01 GM080670Wellcome Trust
6 · The paper itself

Abstract

Protein modifications regulate both DNA repair levels and pathway choice. How each modification achieves regulatory effects and how different modifications collaborate with each other are important questions to be answered. Here, we show that sumoylation regulates double-strand break repair partly by modifying the end resection factor Sae2. This modification is conserved from yeast to humans, and is induced by DNA damage. We mapped the sumoylation site of Sae2 to a single lysine in its self-association domain. Abolishing Sae2 sumoylation by mutating this lysine to arginine impaired Sae2 function in the processing and repair of multiple types of DNA breaks. We found that Sae2 sumoylation occurs independently of its phosphorylation, and the two modifications act in synergy to increase soluble forms of Sae2. We also provide evidence that sumoylation of the Sae2-binding nuclease, the Mre11-Rad50-Xrs2 complex, further increases end resection. These findings reveal a novel role for sumoylation in DNA repair by regulating the solubility of an end resection factor. They also show that collaboration between different modifications and among multiple substrates leads to a stronger biological effect.

Indexed as

DNA-Binding ProteinsDNA Breaks, Double-StrandedDNA DamageDNA End-Joining RepairDNA RepairEndodeoxyribonucleasesEndonucleasesExodeoxyribonucleasesHumansPhosphorylationSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSolubilitySumoylationDNA-Binding ProteinsEndodeoxyribonucleasesEndonucleasesExodeoxyribonucleasesMRE11 protein, S cerevisiaeRAD50 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSAE2 protein, S cerevisiaeXRS2 protein, S cerevisiae

Identifiers

PMID25569253
PMCPMC4287433
OpenAlexW2312652906

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.