Evidence map›Paper›PMID 26177013›Full record

ArticleCell cycle (Georgetown, Tex.)2015

Regulation of Elg1 activity by phosphorylation.

Dganit Shkedy, Nishant Singh, Keren Shemesh, Ayelet Amir, Tamar Geiger, Batia Liefshitz, Yaniv Harari, Martin Kupiec

Open access · bronzeAbstract read
In one paragraph

Article in Cell cycle (Georgetown, Tex.), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

11 citing papers in PubMed, 15 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Deubiquitinases and cancer: A snapshot.Critical reviews in oncology/hematology · 2016
    Review
  10. Potential therapeutic applications of plant toxin-ricin in cancer: challenges and advances.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2015
    Review
  11. Phosphorylation of Elg1 regulates its activity.Cell cycle (Georgetown, Tex.) · 2015
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 3 institutions in 2 countries.

Dganit Shkedya Department of Molecular Microbiology and Biotechnology ; Tel Aviv University ; Ramat Aviv , Israel.
Nishant Singha Department of Molecular Microbiology and Biotechnology ; Tel Aviv University ; Ramat Aviv , Israel.
Keren Shemesha Department of Molecular Microbiology and Biotechnology ; Tel Aviv University ; Ramat Aviv , Israel.
Ayelet Amira Department of Molecular Microbiology and Biotechnology ; Tel Aviv University ; Ramat Aviv , Israel.
Tamar Geigerb Department of Human Molecular Genetics and Biochemistry ; Sackler Faculty of Medicine; Tel Aviv University ; Ramat Aviv , Israel.
Batia Liefshitza Department of Molecular Microbiology and Biotechnology ; Tel Aviv University ; Ramat Aviv , Israel.
Yaniv Hararia Department of Molecular Microbiology and Biotechnology ; Tel Aviv University ; Ramat Aviv , Israel.
Martin Kupieca Department of Molecular Microbiology and Biotechnology ; Tel Aviv University ; Ramat Aviv , Israel.
Alzheimer's Association of Israel · ILTel Aviv University · ILArthur M. Sackler Gallery · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

ELG1 is a conserved gene with important roles in the maintenance of genome stability. Elg1's activity prevents gross chromosomal rearrangements, maintains proper telomere length regulation, helps repairing DNA damage created by a number of genotoxins and participates in sister chromatid cohesion. Elg1 is evolutionarily conserved, and its Fanconi Anemia-related mammalian ortholog (also known as ATAD5) is embryonic lethal when lost in mice and acts as a tumor suppressor in mice and humans. Elg1 encodes a protein that forms an RFC-like complex that unloads the replicative clamp, PCNA, from DNA, mainly in its SUMOylated form. We have identified 2 different regions in yeast Elg1 that undergo phosphorylation. Phosphorylation of one of them, S112, is dependent on the ATR yeast ortholog, Mec1, and probably is a direct target of this kinase. We show that phosphorylation of Elg1 is important for its role at telomeres. Mutants unable to undergo phosphorylation suppress the DNA damage sensitivity of Δrad5 mutants, defective for an error-free post-replicational bypass pathway. This indicates a role of phosphorylation in the regulation of DNA repair. Our results open the way to investigate the mechanisms by which the activity of Elg1 is regulated during DNA replication and in response to DNA damage.

Indexed as

Gene Expression RegulationCarrier ProteinsDNA DamageDNA RepairIntracellular Signaling Peptides and ProteinsMass SpectrometryMethyl MethanesulfonatePhosphorylationProtein Serine-Threonine KinasesSaccharomyces cerevisiae ProteinsTelomereTelomere HomeostasisCarrier ProteinsElg1 protein, S cerevisiaeIntracellular Signaling Peptides and ProteinsMEC1 protein, S cerevisiaeMethyl MethanesulfonateProtein Serine-Threonine KinasesSaccharomyces cerevisiae ProteinsATM/Tel1, ATR/Mec1, DNA damage response, DNA repair, DNA replication, telomeres

Identifiers

PMID26177013
PMCPMC4825795
OpenAlexW871441387

What OpenQuestion holds

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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.