Evidence map›Paper›PMID 25263559›Full record

ArticleCell reports2014

A versatile scaffold contributes to damage survival via sumoylation and nuclease interactions.

Prabha Sarangi, Veronika Altmannova, Cory Holland, Zdenka Bartosova, Fanfan Hao, Dorothea Anrather, Gustav Ammerer, Sang Eun Lee, Lumir Krejci, Xiaolan Zhao

Abstract read
In one paragraph

Article in Cell reports, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Review
  7. A new MCM modification cycle regulates DNA replication initiation.Nature structural & molecular biology · 2016
    Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. 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

10 authors.

Prabha SarangiMolecular Biology Program, Memorial Sloan-Kettering Cancer Center, New York, NY 10065, USA; Programs in Biochemistry, Cell, and Molecular Biology, Weill Cornell Graduate School of Medical Sciences, New York, NY 10065, USA.
Veronika AltmannovaDepartment of Biology, Masaryk University, Brno 62500, Czech Republic.
Cory HollandDepartment of Molecular Medicine, Institute of Biotechnology, University of Texas Health Science Center at San Antonio, San Antonio, TX 78229, USA.
Zdenka BartosovaDepartment of Biology, Masaryk University, Brno 62500, Czech Republic.
Fanfan HaoMolecular Biology Program, Memorial Sloan-Kettering Cancer Center, New York, NY 10065, USA.
Dorothea AnratherDepartment of Biochemistry and Cell Biology, Max F. Perutz Laboratories, University of Vienna, Vienna 1030, Austria.
Gustav AmmererDepartment of Biochemistry and Cell Biology, Max F. Perutz Laboratories, University of Vienna, Vienna 1030, Austria.
Sang Eun LeeDepartment of Molecular Medicine, Institute of Biotechnology, University of Texas Health Science Center at San Antonio, San Antonio, TX 78229, USA; Division of Radiation Biology, Department of Radiation Oncology, University of Texas Health Science Center at San Antonio, San Antonio, TX 78229, USA.
Lumir KrejciDepartment of Biology, Masaryk University, Brno 62500, Czech Republic; National Centre for Biomolecular Research, Masaryk University, Brno 62500, Czech Republic; International Clinical Research Center, St. Anne's University Hospital in Brno, Brno 60200, Czech Republic. Electronic address: lkrejci@chemi.muni.cz.
Xiaolan ZhaoMolecular Biology Program, Memorial Sloan-Kettering Cancer Center, New York, NY 10065, USA; Programs in Biochemistry, Cell, and Molecular Biology, Weill Cornell Graduate School of Medical Sciences, New York, NY 10065, USA. Electronic address: zhaox1@mskcc.org.

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
Mechanisms of Error Prone Repair of DNA BreaksR01GM071011 · NIGMS · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI LEE, SANG EUN · 2004 to 2021
$4.5M
NCI NIH HHS P30 CA008748NIGMS NIH HHS GM071011NIGMS NIH HHS GM080670NIGMS NIH HHS R01 GM071011NIGMS NIH HHS R01 GM080670
6 · The paper itself

Abstract

DNA repair scaffolds mediate specific DNA and protein interactions in order to assist repair enzymes in recognizing and removing damaged sequences. Many scaffold proteins are dedicated to repairing a particular type of lesion. Here, we show that the budding yeast Saw1 scaffold is more versatile. It helps cells cope with base lesions and protein-DNA adducts through its known function of recruiting the Rad1-Rad10 nuclease to DNA. In addition, it promotes UV survival via a mechanism mediated by its sumoylation. Saw1 sumoylation favors its interaction with another nuclease Slx1-Slx4, and this SUMO-mediated role is genetically separable from two main UV lesion repair processes. These effects of Saw1 and its sumoylation suggest that Saw1 is a multifunctional scaffold that can facilitate diverse types of DNA repair through its modification and nuclease interactions.

Indexed as

DNA DamageDNA RepairDNA-Binding ProteinsEndonucleasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSumoylationSurvival AnalysisDNA-Binding ProteinsEndonucleasesSaccharomyces cerevisiae ProteinsSaw1 protein, S cerevisiae

Identifiers

PMID25263559
PMCPMC4280569

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.