Evidence map›Paper›PMID 25189701›Full record

ArticleGenes & development2014

A quantitative 14-3-3 interaction screen connects the nuclear exosome targeting complex to the DNA damage response.

Melanie Blasius, Sebastian A Wagner, Chunaram Choudhary, Jiri Bartek, Stephen P Jackson

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
–field-weighted citation impact
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

36 citing papers in PubMed, 56 citations in OpenAlex.

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  14. Review
  15. Controlling nuclear RNA levels.Nature reviews. Genetics · 2018
    Review
  16. Article
  17. Structural basis for MTR4-ZCCHC8 interactions that stimulate the MTR4 helicase in the nuclear exosome-targeting complex.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  18. 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

5 authors at 4 institutions in 3 countries.

Melanie BlasiusThe Gurdon Institute, Department of Biochemistry, University of Cambridge, Cambridge CB2 1QN, United Kingdom; Genome Integrity Unit, Danish Cancer Society Research Centre, 2100 Copenhagen, Denmark;
Sebastian A WagnerThe Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, 2200 Copenhagen, Denmark;
Chunaram ChoudharyThe Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, 2200 Copenhagen, Denmark;
Jiri BartekThe Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, 2200 Copenhagen, Denmark; Institute of Molecular and Translational Medicine, Palacky University, 77900 Olomouc, Czech Republic;
Stephen P JacksonThe Gurdon Institute, Department of Biochemistry, University of Cambridge, Cambridge CB2 1QN, United Kingdom; The Wellcome Trust Sanger Institute, Hinxton, Cambridge CB10 1SA, United Kingdom s.jackson@gurdon.cam.ac.uk jb@cancer.dk.
Novo Nordisk Foundation · DKDanish Cancer Society · DKInstitute of Molecular and Translational Medicine · CZWellcome Sanger Institute · GB

Funding

Cancer Research UK 11224Cancer Research UK C6946/A14492Cancer Research UK C6/A11224Wellcome Trust 092096
6 · The paper itself

Abstract

RNA metabolism is altered following DNA damage, but the underlying mechanisms are not well understood. Through a 14-3-3 interaction screen for DNA damage-induced protein interactions in human cells, we identified protein complexes connected to RNA biology. These include the nuclear exosome targeting (NEXT) complex that regulates turnover of noncoding RNAs termed promoter upstream transcripts (PROMPTs). We show that the NEXT subunit RBM7 is phosphorylated upon DNA damage by the MAPKAPK2 kinase and establish that this mediates 14-3-3 binding and decreases PROMPT binding. These findings and our observation that cells lacking RBM7 display DNA damage hypersensitivity link PROMPT turnover to the DNA damage response.

Indexed as

14-3-3 ProteinsDNA DamageExosome Multienzyme Ribonuclease ComplexHumansIntracellular Signaling Peptides and ProteinsMAP-Kinase-Activated Kinase 2MAP Kinase Signaling SystemPhosphorylationProtein BindingProtein Serine-Threonine KinasesRNA, UntranslatedUltraviolet Rays14-3-3 ProteinsExosome Multienzyme Ribonuclease ComplexIntracellular Signaling Peptides and ProteinsMAP-Kinase-Activated Kinase 2Protein Serine-Threonine KinasesRNA, Untranslated14-3-3DNA damage responseMAPKAPK2nuclear exosomeUV

Identifiers

PMID25189701
PMCPMC4173157
OpenAlexW2073364366

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.