Evidence map›Paper›PMID 25414343›Full record

ArticleNucleic acids research2014

Identification by high-throughput imaging of the histone methyltransferase EHMT2 as an epigenetic regulator of VEGFA alternative splicing.

Maayan Salton, Ty C Voss, Tom Misteli

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 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

29 citing papers in PubMed, 53 citations in OpenAlex.

  1. Article
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  13. Article
  14. Histone methylation and vascular biology.Clinical epigenetics · 2020
    Review
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Report and Application of a Tool Compound Data Set.Journal of chemical information and modeling · 2017
    Article
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

3 authors at 1 institution in 1 country.

Maayan SaltonNational Cancer Institute, NIH, Bethesda, MD 20892, USA maayan.salton@gmail.com.
Ty C VossNational Cancer Institute, NIH, Bethesda, MD 20892, USA.
Tom MisteliNational Cancer Institute, NIH, Bethesda, MD 20892, USA mistelit@mail.nih.gov.
National Cancer Institute · US

Funding

Nuclear Architecture and DiseaseZIABC010309 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI MISTELI, THOMAS A · 2009 to 2025
$39.8M
Intramural NIH HHS
6 · The paper itself

Abstract

Recent evidence points to a role of chromatin in regulation of alternative pre-mRNA splicing (AS). In order to identify novel chromatin regulators of AS, we screened an RNAi library of chromatin proteins using a cell-based high-throughput in vivo assay. We identified a set of chromatin proteins that regulate AS. Using simultaneous genome-wide expression and AS analysis, we demonstrate distinct and non-overlapping functions of these chromatin modifiers on transcription and AS. Detailed mechanistic characterization of one dual function chromatin modifier, the H3K9 methyltransferase EHMT2 (G9a), identified VEGFA as a major chromatin-mediated AS target. Silencing of EHMT2, or its heterodimer partner EHMT1, affects AS by promoting exclusion of VEGFA exon 6a, but does not alter total VEGFA mRNA levels. The epigenetic regulatory mechanism of AS by EHMT2 involves an adaptor system consisting of the chromatin modulator HP1γ, which binds methylated H3K9 and recruits splicing regulator SRSF1. The epigenetic regulation of VEGFA is physiologically relevant since EHMT2 is transcriptionally induced in response to hypoxia and triggers concomitant changes in AS of VEGFA. These results characterize a novel epigenetic regulatory mechanism of AS and they demonstrate separate roles of epigenetic modifiers in transcription and alternative splicing.

Indexed as

Alternative SplicingEpigenesis, GeneticCell HypoxiaCell Line, TumorChromatinChromosomal Proteins, Non-HistoneHEK293 CellsHistocompatibility AntigensHistone-Lysine N-MethyltransferaseHumansMCF-7 CellsMicroscopy, FluorescenceNuclear ProteinsRNA-Binding ProteinsRNA InterferenceSerine-Arginine Splicing FactorsCBX3 protein, humanChromatinChromosomal Proteins, Non-HistoneEHMT2 protein, humanHistocompatibility AntigensHistone-Lysine N-MethyltransferaseNuclear ProteinsRNA-Binding ProteinsSerine-Arginine Splicing FactorsVascular Endothelial Growth Factor AVEGFA protein, human

Identifiers

PMID25414343
PMCPMC4267647
OpenAlexW2110264114

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.