Evidence map›Paper›PMID 27849008›Full record

ArticleScientific reports2016

Ku70 Serine 155 mediates Aurora B inhibition and activation of the DNA damage response.

Victoria L Fell, Elizabeth A Walden, Sarah M Hoffer, Stephanie R Rogers, Amelia S Aitken, Louisa M Salemi, Caroline Schild-Poulter

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

9 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
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  7. Regulation of c-Raf Stability through the CTLH Complex.International journal of molecular sciences · 2019
    Article
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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

7 authors at 1 institution in 1 country.

Victoria L FellRobarts Research Institute and Department of Biochemistry, Schulich School of Medicine &Dentistry, The University of Western Ontario, London, Ontario N6A 5B7, Canada.
Elizabeth A WaldenRobarts Research Institute and Department of Biochemistry, Schulich School of Medicine &Dentistry, The University of Western Ontario, London, Ontario N6A 5B7, Canada.
Sarah M HofferRobarts Research Institute and Department of Biochemistry, Schulich School of Medicine &Dentistry, The University of Western Ontario, London, Ontario N6A 5B7, Canada.
Stephanie R RogersRobarts Research Institute and Department of Biochemistry, Schulich School of Medicine &Dentistry, The University of Western Ontario, London, Ontario N6A 5B7, Canada.
Amelia S AitkenRobarts Research Institute and Department of Biochemistry, Schulich School of Medicine &Dentistry, The University of Western Ontario, London, Ontario N6A 5B7, Canada.
Louisa M SalemiRobarts Research Institute and Department of Biochemistry, Schulich School of Medicine &Dentistry, The University of Western Ontario, London, Ontario N6A 5B7, Canada.
Caroline Schild-PoulterRobarts Research Institute and Department of Biochemistry, Schulich School of Medicine &Dentistry, The University of Western Ontario, London, Ontario N6A 5B7, Canada.
Western University · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Ku heterodimer (Ku70/Ku80) is the central DNA binding component of the classical non-homologous end joining (NHEJ) pathway that repairs DNA double-stranded breaks (DSBs), serving as the scaffold for the formation of the NHEJ complex. Here we show that Ku70 is phosphorylated on Serine 155 in response to DNA damage. Expression of Ku70 bearing a S155 phosphomimetic substitution (Ku70 S155D) in Ku70-deficient mouse embryonic fibroblasts (MEFs) triggered cell cycle arrest at multiple checkpoints and altered expression of several cell cycle regulators in absence of DNA damage. Cells expressing Ku70 S155D exhibited a constitutive DNA damage response, including ATM activation, H2AX phosphorylation and 53BP1 foci formation. Ku70 S155D was found to interact with Aurora B and to have an inhibitory effect on Aurora B kinase activity. Lastly, we demonstrate that Ku and Aurora B interact following ionizing radiation treatment and that Aurora B inhibition in response to DNA damage is dependent upon Ku70 S155 phosphorylation. This uncovers a new pathway where Ku may relay signaling to Aurora B to enforce cell cycle arrest in response to DNA damage.

Indexed as

DNA DamageDNA RepairAnimalsAurora Kinase BCell Cycle CheckpointsCells, CulturedCell SurvivalDNA Breaks, Double-StrandedEmbryo, MammalianFibroblastsKu AutoantigenMice, KnockoutPhosphorylationProtein BindingRadiation, IonizingSerineAurora Kinase BKu AutoantigenSerine

Identifiers

PMID27849008
PMCPMC5111114
OpenAlexW2549998226

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.