Evidence map›Paper›PMID 25599992›Full record

ArticleThe EMBO journal2015

Nuclear matrix protein Matrin3 regulates alternative splicing and forms overlapping regulatory networks with PTB.

Miguel B Coelho, Jan Attig, Nicolás Bellora, Julian König, Martina Hallegger, Melis Kayikci, Eduardo Eyras, Jernej Ule, Christopher W J Smith

Open access · hybridAbstract read
In one paragraph

Article in The EMBO journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 101 papers.

0numbers the graph read from it
0cells of the map it votes in
101citing papers in PubMed
7.8field-weighted citation impact, top 2% 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

101 citing papers in PubMed, 163 citations in OpenAlex.

  1. Article
  2. Review
  3. MATR3 regulates METTL3-Mediated mJournal of bioenergetics and biomembranes · 2026
    Article
  4. Article
  5. Article
  6. Allele-specific splicing modulates protein isoforms and Alzheimer's risk.bioRxiv : the preprint server for biology · 2026
    Article
  7. Article
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  12. Article
  13. Article
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  15. Article
  16. Review
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  18. Surface PD-1 expression in T cells is suppressed by HNRNPK through an exonic splicing silencer on exon 3.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2024
    Article
  19. Review
  20. Review

41 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

9 authors at 5 institutions in 3 countries.

Miguel B CoelhoDepartment of Biochemistry, University of Cambridge, Cambridge, UK.
Jan AttigDepartment of Molecular Neuroscience, UCL Institute of Neurology, London, UK MRC-Laboratory of Molecular Biology, Cambridge, UK.
Nicolás BelloraComputational Genomics, Universitat Pompeu Fabra, Barcelona, Spain Catalan Institute for Research and Advanced Studies (ICREA), Barcelona, Spain INIBIOMA CONICET-UNComahue, Bariloche, Argentina.
Julian KönigMRC-Laboratory of Molecular Biology, Cambridge, UK.
Martina HalleggerDepartment of Biochemistry, University of Cambridge, Cambridge, UK Department of Molecular Neuroscience, UCL Institute of Neurology, London, UK.
Melis KayikciMRC-Laboratory of Molecular Biology, Cambridge, UK.
Eduardo EyrasComputational Genomics, Universitat Pompeu Fabra, Barcelona, Spain Catalan Institute for Research and Advanced Studies (ICREA), Barcelona, Spain.
Jernej UleDepartment of Molecular Neuroscience, UCL Institute of Neurology, London, UK.
Christopher W J SmithDepartment of Biochemistry, University of Cambridge, Cambridge, UK cwjs1@cam.ac.uk.
University of Cambridge · GBMRC Laboratory of Molecular Biology · GBUniversity College London · GBNational University of Comahue · ARPompeu Fabra University · ES

Funding

Medical Research Council MC_U105185858Wellcome Trust 077877Wellcome Trust 089701Wellcome Trust 092900
6 · The paper itself

Abstract

Matrin3 is an RNA- and DNA-binding nuclear matrix protein found to be associated with neural and muscular degenerative diseases. A number of possible functions of Matrin3 have been suggested, but no widespread role in RNA metabolism has yet been clearly demonstrated. We identified Matrin3 by its interaction with the second RRM domain of the splicing regulator PTB. Using a combination of RNAi knockdown, transcriptome profiling and iCLIP, we find that Matrin3 is a regulator of hundreds of alternative splicing events, principally acting as a splicing repressor with only a small proportion of targeted events being co-regulated by PTB. In contrast to other splicing regulators, Matrin3 binds to an extended region within repressed exons and flanking introns with no sharply defined peaks. The identification of this clear molecular function of Matrin3 should help to clarify the molecular pathology of ALS and other diseases caused by mutations of Matrin3.

Indexed as

Alternative SplicingComputational BiologyDNA PrimersElectrophoresis, Polyacrylamide GelGene Expression ProfilingGene Regulatory NetworksHEK293 CellsHeLa CellsHumansMicroarray AnalysisNuclear Matrix-Associated ProteinsPolypyrimidine Tract-Binding ProteinReverse Transcriptase Polymerase Chain ReactionRNA-Binding ProteinsRNA InterferenceRNA, Small InterferingDNA PrimersMATR3 protein, humanNuclear Matrix-Associated ProteinsPolypyrimidine Tract-Binding ProteinRNA-Binding ProteinsRNA, Small Interferingalternative splicingMatrin3PTB

Identifiers

PMID25599992
PMCPMC4365034
OpenAlexW2167035187

What OpenQuestion holds

Textmetadata
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.