Evidence map›Paper›PMID 27924002›Full record

ArticleNucleic acids research2017

SFPQ•NONO and XLF function separately and together to promote DNA double-strand break repair via canonical nonhomologous end joining.

Lahcen Jaafar, Zhentian Li, Shuyi Li, William S Dynan

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

63 citing papers in PubMed, 99 citations in OpenAlex.

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3 more citing papers are in PubMed but not listed here.

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

4 authors at 1 institution in 1 country.

Lahcen JaafarDepartments of Radiation Oncology and Biochemistry, Emory University, Atlanta, GA 30322, USA.
Zhentian LiDepartments of Radiation Oncology and Biochemistry, Emory University, Atlanta, GA 30322, USA.
Shuyi LiDepartments of Radiation Oncology and Biochemistry, Emory University, Atlanta, GA 30322, USA.
William S DynanDepartments of Radiation Oncology and Biochemistry, Emory University, Atlanta, GA 30322, USA.
Emory University · US

Funding

Regulation of DNA Double-Strand Break RepairR01CA098239 · NCI · MEDICAL COLLEGE OF GEORGIA (MCG) · PI DYNAN, WILLIAM S. · 2004 to 2013
$2.1M
NCI NIH HHS R01 CA098239
6 · The paper itself

Abstract

A complex of two related mammalian proteins, SFPQ and NONO, promotes DNA double-strand break repair via the canonical nonhomologous end joining (c-NHEJ) pathway. However, its mechanism of action is not fully understood. Here we describe an improved SFPQ•NONO-dependent in vitro end joining assay. We use this system to demonstrate that the SFPQ•NONO complex substitutes in vitro for the core c-NHEJ factor, XLF. Results are consistent with a model where SFPQ•NONO promotes sequence-independent pairing of DNA substrates, albeit in a way that differs in detail from XLF. Although SFPQ•NONO and XLF function redundantly in vitro, shRNA-mediated knockdown experiments indicate that NONO and XLF are both required for efficient end joining and radioresistance in cell-based assays. In addition, knockdown of NONO sensitizes cells to the interstrand crosslinking agent, cisplatin, whereas knockdown of XLF does not, and indeed suppresses the effect of NONO deficiency. These findings suggest that each protein has one or more unique activities, in addition to the DNA pairing revealed in vitro, that contribute to DNA repair in the more complex cellular milieu. The SFPQ•NONO complex contains an RNA binding domain, and prior work has demonstrated diverse roles in RNA metabolism. It is thus plausible that the additional repair function of NONO, revealed in cell-based assays, could involve RNA interaction.

Indexed as

DNA Breaks, Double-StrandedDNA End-Joining RepairDNA RepairCell LineCell SurvivalDNA-Binding ProteinsDNA Repair EnzymesEpistasis, GeneticHumansNuclear Matrix-Associated ProteinsOctamer Transcription FactorsProtein BindingProtein Interaction Domains and MotifsPTB-Associated Splicing FactorRNA-Binding ProteinsDNA-Binding ProteinsDNA Repair EnzymesNHEJ1 protein, humanNONO protein, humanNuclear Matrix-Associated ProteinsOctamer Transcription FactorsPTB-Associated Splicing FactorRNA-Binding Proteins

Identifiers

PMID27924002
PMCPMC5605232
OpenAlexW2588101937

What OpenQuestion holds

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LicenceCC BY-NC
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.