Evidence map›Paper›PMID 21205864›Full record

ArticleGenes & development2011

Functional antagonism between histone H3K4 demethylases in vivo.

Luisa Di Stefano, James A Walker, Giosalba Burgio, Davide F V Corona, Peter Mulligan, Anders M Näär, Nicholas J Dyson

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing 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

35 citing papers in PubMed, 74 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Epigenetic Mechanisms of Alcohol Neuroadaptation: Insights fromJournal of experimental neuroscience · 2018
    Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. Review
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

7 authors at 4 institutions in 2 countries.

Luisa Di StefanoMassachusetts General Hospital Cancer Center, Harvard Medical School, Charlestown, Massachusetts 02129, USA.
James A Walker
Giosalba Burgio
Davide F V Corona
Peter Mulligan
Anders M Näär
Nicholas J Dyson
Harvard University · USMassachusetts General Hospital · USUniversity of Palermo · ITCenter for Human Genetics · US

Funding

The E2F/RBF networkR01GM053203 · NIGMS · MASSACHUSETTS GENERAL HOSPITAL · PI DYSON, NICHOLAS J · 1995 to 2010
$4.2M
MUTAGENESIS OF THE PRB POCKET DOMAINR01CA064402 · NCI · MASSACHUSETTS GENERAL HOSPITAL · PI DYSON, NICHOLAS J · 1994 to 2015
$4.1M
Activator-Targeted Subunits of the ARC/MediatorR01GM071449 · NIGMS · MASSACHUSETTS GENERAL HOSPITAL · PI NAAR, ANDERS M · 2005 to 2010
$1.8M
The Enhancement and Suppression of E2F-Dependent ApoptosisR01GM081607 · NIGMS · MASSACHUSETTS GENERAL HOSPITAL · PI DYSON, NICHOLAS J · 2008 to 2011
$1.3M
NCI NIH HHS CA64402NCI NIH HHS R01 CA064402NIGMS NIH HHS GM071449NIGMS NIH HHS GM53203NIGMS NIH HHS GM81607NIGMS NIH HHS R01 GM053203NIGMS NIH HHS R01 GM071449NIGMS NIH HHS R01 GM081607Telethon TCR09002
6 · The paper itself

Abstract

Dynamic regulation of histone modifications is critical during development, and aberrant activity of chromatin-modifying enzymes has been associated with diseases such as cancer. Histone demethylases have been shown to play a key role in eukaryotic gene transcription; however, little is known about how their activities are coordinated in vivo to regulate specific biological processes. In Drosophila, two enzymes, dLsd1 (Drosophila ortholog of lysine-specific demethylase 1) and Lid (little imaginal discs), demethylate histone H3 at Lys 4 (H3K4), a residue whose methylation is associated with actively transcribed genes. Our studies show that compound mutation of Lid and dLsd1 results in increased H3K4 methylation levels. However, unexpectedly, Lid mutations strongly suppress dLsd1 mutant phenotypes. Investigation of the basis for this antagonism revealed that Lid opposes the functions of dLsd1 and the histone methyltransferase Su(var)3-9 in promoting heterochromatin spreading at heterochromatin-euchromatin boundaries. Moreover, our data reveal a novel role for dLsd1 in Notch signaling in Drosophila, and a complex network of interactions between dLsd1, Lid, and Notch signaling at euchromatic genes. These findings illustrate the complexity of functional interplay between histone demethylases in vivo, providing insights into the epigenetic regulation of heterochromatin/euchromatin boundaries by Lid and dLsd1 and showing their involvement in Notch pathway-specific control of gene expression in euchromatin.

Indexed as

AnimalsDrosophila melanogasterDrosophila ProteinsGene Expression RegulationHeterochromatinHistone DemethylasesHistone-Lysine N-MethyltransferaseHistonesMethylationMutationOxidoreductases, N-DemethylatingPhenotypeReceptors, NotchSignal TransductionDrosophila ProteinsHeterochromatinHistone DemethylasesHistone-Lysine N-MethyltransferaseHistonesLid protein, DrosophilaLsd-1 protein, DrosophilaOxidoreductases, N-DemethylatingReceptors, Notch

Identifiers

PMID21205864
PMCPMC3012933
OpenAlexW2034884441

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.