Evidence map›Paper›PMID 24567323›Full record

ArticleThe Journal of biological chemistry2014

Regulation of Ku-DNA association by Yku70 C-terminal tail and SUMO modification.

Lisa E Hang, Christopher R Lopez, Xianpeng Liu, Jaime M Williams, Inn Chung, Lei Wei, Alison A Bertuch, Xiaolan Zhao

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed, 1 pooled it
2.3field-weighted citation impact, top 12% 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

23 citing papers in PubMed, 1 synthesis or guideline pooled it, 31 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Article
  4. Article
  5. Review
  6. The Multifaceted Roles of Ku70/80.International journal of molecular sciences · 2021
    Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. SUMO, a small, but powerful, regulator of double-strand break repair.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017
    Review
  14. Article
  15. Review
  16. Roles of SUMO in Replication Initiation, Progression, and Termination.Advances in experimental medicine and biology · 2017
    Review
  17. Article
  18. Article
  19. 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 3 institutions in 1 country.

Lisa E HangMolecular Biology Program, Memorial Sloan Kettering Cancer Center, New York, New York 10065; Programs in Biochemistry, Cell, and Molecular Biology, Weill Graduate School of Medical Sciences of Cornell University, New York, New York 10065.
Christopher R LopezDepartment of Pediatrics, Baylor College of Medicine, Houston, Texas 77030.
Xianpeng LiuMolecular Biology Program, Memorial Sloan Kettering Cancer Center, New York, New York 10065.
Jaime M WilliamsDepartment of Molecular and Human Genetics, Baylor College of Medicine, Houston, Texas 77030.
Inn ChungMolecular Biology Program, Memorial Sloan Kettering Cancer Center, New York, New York 10065.
Lei WeiMolecular Biology Program, Memorial Sloan Kettering Cancer Center, New York, New York 10065; Gerstner Sloan Kettering Graduate School of Biomedical Sciences, New York, New York 10065.
Alison A BertuchDepartment of Pediatrics, Baylor College of Medicine, Houston, Texas 77030; Department of Molecular and Human Genetics, Baylor College of Medicine, Houston, Texas 77030.
Xiaolan ZhaoMolecular Biology Program, Memorial Sloan Kettering Cancer Center, New York, New York 10065; Programs in Biochemistry, Cell, and Molecular Biology, Weill Graduate School of Medical Sciences of Cornell University, New York, New York 10065; Gerstner Sloan Kettering Graduate School of Biomedical Sciences, New York, New York 10065. Electronic address: zhaox1@mskcc.org.
Baylor College of Medicine · USMemorial Sloan Kettering Cancer Center · USCornell University · US

Funding

X-RAY CRYSTALLOGRAPHYP30CA008748 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI Nicholas D Socci · 1985 to 2026
$347.4M
PROGRAM IN HUMAN MOLECULAR GENETICST32GM008307 · NIGMS · BAYLOR COLLEGE OF MEDICINE · PI SHAULSKY, GAD · 1990 to 2020
$6.6M
The Rtt107 interactome structures and functionsR01GM080670 · NIGMS · SLOAN-KETTERING INST CAN RESEARCH · PI ZHAO, XIAOLAN · 2007 to 2021
$4.5M
The Roles of the Ku Heterodimer in Yeast Telomere FunctionR01GM077509 · NIGMS · BAYLOR COLLEGE OF MEDICINE · PI BERTUCH, ALISON A · 2007 to 2018
$3.0M
NCI NIH HHS P30 CA008748NIGMS NIH HHS GM077509NIGMS NIH HHS GM080670NIGMS NIH HHS R01 GM077509NIGMS NIH HHS R01 GM080670NIGMS NIH HHS T32 GM008307
6 · The paper itself

Abstract

The Ku70-Ku80 ring complex encloses DNA ends to facilitate telomere maintenance and DNA break repair. Many studies focus on the ring-forming regions of subunits Ku70 and Ku80. Less is known about the Ku70 C-terminal tail, which lies outside the ring. Our results suggest that this region is responsible for dynamic sumoylation of Yku70 upon DNA association in budding yeast. Mutating a cluster of five lysines in this region largely eliminates Yku70 sumoylation. Chromatin immunoprecipitation analyses show that yku70 mutants with these lysines replaced by arginines exhibit reduced Ku-DNA association at both telomeres and internal DNA breaks. Consistent with this physical evidence, Yku70 sumoylation deficiency is associated with impaired ability to block DNA end resection and suppression of multiple defects caused by inefficient resection. Correlating with these, yku70 mutants with reduced sumoylation levels exhibit shorter telomeres, increased G overhang levels, and altered levels of non-homologous end joining. We also show that diminution of sumoylation does not affect Yku70 protein levels or its interactions with protein and RNA partners. These results suggest a model whereby Yku70 sumoylation upon DNA association strengthens Ku-DNA interaction to promote multiple functions of Ku.

Indexed as

DNADNA-Binding ProteinsDNA End-Joining RepairDNA RepairGene Expression Regulation, FungalLysineMutationNuclear ProteinsPhenotypePlasmidsProtein BindingProtein Structure, TertiarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSumoylationTelomereDNADNA-Binding ProteinsLysineNuclear ProteinsSaccharomyces cerevisiae ProteinsYKU70 protein, S cerevisiaeDNA RepairKu ComplexMolecular GeneticsSumoylationTelomeresYeast

Identifiers

PMID24567323
PMCPMC4036155
OpenAlexW2052104137

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.