Evidence map›Paper›PMID 25428364›Full record

ArticleNucleic acids research2014

Abundance of the Fanconi anaemia core complex is regulated by the RuvBL1 and RuvBL2 AAA+ ATPases.

Eeson Rajendra, Juan I Garaycoechea, Ketan J Patel, Lori A Passmore

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

26 citing papers in PubMed, 48 citations in OpenAlex.

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  5. Epigenetic Control of Translation Checkpoint and Tumor Progression via RUVBL1-EEF1A1 Axis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023
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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

4 authors at 2 institutions in 1 country.

Eeson RajendraMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, CB2 0QH, UK.
Juan I GaraycoecheaMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, CB2 0QH, UK.
Ketan J PatelMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, CB2 0QH, UK Department of Medicine, Level 5, Addenbrooke's Hospital, University of Cambridge, Cambridge, CB2 0QQ, UK.
Lori A PassmoreMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, CB2 0QH, UK passmore@mrc-lmb.cam.ac.uk.
MRC Laboratory of Molecular Biology · GBUniversity of Cambridge · GB

Funding

Cancer Research UK 13647Medical Research Council MC U105178811Medical Research Council MC_U105178811Medical Research Council MC U105192715Medical Research Council MC_U105192715
6 · The paper itself

Abstract

Fanconi anaemia (FA) is a genome instability disease caused by defects in the FA DNA repair pathway that senses and repairs damage caused by DNA interstrand crosslinks. At least 8 of the 16 genes found mutated in FA encode proteins that assemble into the FA core complex, a multisubunit monoubiquitin E3 ligase. Here, we show that the RuvBL1 and RuvBL2 AAA+ ATPases co-purify with FA core complex isolated under stringent but native conditions from a vertebrate cell line. Depletion of the RuvBL1-RuvBL2 complex in human cells causes hallmark features of FA including DNA crosslinker sensitivity, chromosomal instability and defective FA pathway activation. Genetic knockout of RuvBL1 in a murine model is embryonic lethal while conditional inactivation in the haematopoietic stem cell pool confers profound aplastic anaemia. Together these findings reveal a function for RuvBL1-RuvBL2 in DNA repair through a physical and functional association with the FA core complex. Surprisingly, depletion of RuvBL1-RuvBL2 leads to co-depletion of the FA core complex in human cells. This suggests that a potential mechanism for the role of RuvBL1-RuvBL2 in maintaining genome integrity is through controlling the cellular abundance of FA core complex.

Indexed as

Adenosine TriphosphatasesAnemia, AplasticAnimalsAtaxia Telangiectasia Mutated ProteinsATPases Associated with Diverse Cellular ActivitiesCarrier ProteinsCell LineChickensCross-Linking ReagentsDNA HelicasesFanconi Anemia Complementation Group ProteinsHematopoietic Stem CellsHumansMice, KnockoutSignal TransductionAdenosine TriphosphatasesAtaxia Telangiectasia Mutated ProteinsATPases Associated with Diverse Cellular ActivitiesATR protein, humanCarrier ProteinsCross-Linking ReagentsDNA HelicasesFanconi Anemia Complementation Group ProteinsRUVBL1 protein, humanRUVBL1 protein, mouseRUVBL2 protein, human

Identifiers

PMID25428364
PMCPMC4267650
OpenAlexW2015626135

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.