Evidence map›Paper›PMID 25525152›Full record

ArticleRNA (New York, N.Y.)2015

p38MAPK/MK2-mediated phosphorylation of RBM7 regulates the human nuclear exosome targeting complex.

Christopher Tiedje, Michal Lubas, Mohammad Tehrani, Manoj B Menon, Natalia Ronkina, Simon Rousseau, Philip Cohen, Alexey Kotlyarov, Matthias Gaestel

Open access · bronzeAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

25 citing papers in PubMed, 43 citations in OpenAlex.

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  15. Controlling nuclear RNA levels.Nature reviews. Genetics · 2018
    Review
  16. 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
  17. 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

9 authors at 3 institutions in 3 countries.

Christopher TiedjeInstitute of Physiological Chemistry, Hannover Medical School, 30625 Hannover, Germany Tiedje.Christopher@mh-hannover.de Gaestel.Matthias@mh-hannover.de.
Michal LubasCentre for mRNP Biogenesis and Metabolism, Department of Molecular Biology and Genetics, Aarhus University, DK-8000 Aarhus C, Denmark.
Mohammad TehraniInstitute of Physiological Chemistry, Hannover Medical School, 30625 Hannover, Germany.
Manoj B MenonInstitute of Physiological Chemistry, Hannover Medical School, 30625 Hannover, Germany.
Natalia RonkinaInstitute of Physiological Chemistry, Hannover Medical School, 30625 Hannover, Germany.
Simon RousseauMRC Phosphorylation und Ubiquitylation Unit (MRC-PPU), Dundee, Scotland DD1 5EH, United Kingdom.
Philip CohenMRC Phosphorylation und Ubiquitylation Unit (MRC-PPU), Dundee, Scotland DD1 5EH, United Kingdom.
Alexey KotlyarovInstitute of Physiological Chemistry, Hannover Medical School, 30625 Hannover, Germany.
Matthias GaestelInstitute of Physiological Chemistry, Hannover Medical School, 30625 Hannover, Germany Tiedje.Christopher@mh-hannover.de Gaestel.Matthias@mh-hannover.de.
Medizinische Hochschule Hannover · DEMRC Protein Phosphorylation and Ubiquitylation Unit · GBAarhus University · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The nuclear exosome targeting complex (NEXT) directs a major 3'-5' exonuclease, the RNA exosome, for degradation of nuclear noncoding (nc) RNAs. We identified the RNA-binding component of the NEXT complex, RBM7, as a substrate of p38(MAPK)/MK2-mediated phosphorylation at residue S136. As a result of this phosphorylation, RBM7 displays a strongly decreased RNA-binding capacity, while inhibition of p38(MAPK) or mutation of S136A in RBM7 increases its RNA association. Interestingly, promoter-upstream transcripts (PROMPTs), such as proRBM39, proEXT1, proDNAJB4, accumulated upon stress stimulation in a p38(MAPK)/MK2-dependent manner, a process inhibited by overexpression of RBM7(S136A). While there are no stress-dependent changes in RNA-polymerase II (RNAPII) occupation of PROMPT regions representing unchanged transcription, stability of PROMPTs is increased. Hence, we propose that phosphorylation of RBM7 by the p38(MAPK)/MK2 axis increases nuclear ncRNA stability by blocking their RBM7-binding and subsequent RNA exosome targeting to allow stress-dependent modulations of the noncoding transcriptome.

Indexed as

Protein Processing, Post-TranslationalCarrier ProteinsCell NucleusExosomesHEK293 CellsHeLa CellsHumansIntracellular Signaling Peptides and ProteinsMAP-Kinase-Activated Kinase 2Multiprotein ComplexesNuclear Proteinsp38 Mitogen-Activated Protein KinasesPhosphorylationProtein BindingProtein Serine-Threonine KinasesRNA-Binding ProteinsCarrier ProteinsIntracellular Signaling Peptides and ProteinsMAP-Kinase-Activated Kinase 2Multiprotein ComplexesNuclear Proteinsp38 Mitogen-Activated Protein KinasesProtein Serine-Threonine KinasesRBM7 protein, humanRNA-Binding ProteinsRNA, UntranslatedZCCHC8 protein, humanncRNAsp38MAPK/MK2 signalingphosphorylationRBM7RNA bindingRNA stability

Identifiers

PMID25525152
PMCPMC4338353
OpenAlexW2133728532

What OpenQuestion holds

Textmetadata
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.