Evidence map›Paper›PMID 23197473›Full record

ArticleMolecular biology of the cell2013

Ash2 acts as an ecdysone receptor coactivator by stabilizing the histone methyltransferase Trr.

Albert Carbonell, Alexander Mazo, Florenci Serras, Montserrat Corominas

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
0.4field-weighted citation impact, top 39% 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

15 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. bioRxiv : the preprint server for biology · 2025
    Article
  3. Loss-of-function in RBBP5 results in a syndromic neurodevelopmental disorder associated with microcephaly.Genetics in medicine : official journal of the American College of Medical Genetics · 2024
    Article
  4. Coregulators Reside withinInternational journal of molecular sciences · 2023
    Article
  5. Article
  6. Article
  7. Review
  8. Direct and widespread role for the nuclear receptor EcR in mediating the response to ecdysone inProceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. 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

4 authors at 2 institutions in 2 countries.

Albert CarbonellDepartament de Genètica and Institut de Biomedicina, Universitat de Barcelona, 08028 Barcelona, Spain.
Alexander Mazo
Florenci Serras
Montserrat Corominas
Universitat de Barcelona · ESThomas Jefferson University · US

Funding

The Role of Epigenetic Factors in Regulation of Coding and Non-Coding HOX GenesP01CA129242 · NCI · OHIO STATE UNIVERSITY · PI ALDER, HANSJUERG · 2009 to 2013
$4.7M
NCI NIH HHS P01 CA129242
6 · The paper itself

Abstract

The molting hormone ecdysone triggers chromatin changes via histone modifications that are important for gene regulation. On hormone activation, the ecdysone receptor (EcR) binds to the SET domain-containing histone H3 methyltransferase trithorax-related protein (Trr). Methylation of histone H3 at lysine 4 (H3K4me), which is associated with transcriptional activation, requires several cofactors, including Ash2. We find that ash2 mutants have severe defects in pupariation and metamorphosis due to a lack of activation of ecdysone-responsive genes. This transcriptional defect is caused by the absence of the H3K4me3 marks set by Trr in these genes. We present evidence that Ash2 interacts with Trr and is required for its stabilization. Thus we propose that Ash2 functions together with Trr as an ecdysone receptor coactivator.

Indexed as

AnimalsDrosophila melanogasterDrosophila ProteinsEcdysoneEnzyme StabilityFemaleGenes, LethalHistone-Lysine N-MethyltransferaseHistonesImaginal DiscsLarvaMaleMethylationNuclear ProteinsPhenotypePolytene Chromosomesash2 protein, DrosophilaDrosophila ProteinsEcdysoneecdysone receptorHistone-Lysine N-MethyltransferaseHistonesNuclear ProteinsReceptors, SteroidTranscription FactorsTRR protein, Drosophila

Identifiers

PMID23197473
PMCPMC3565548
OpenAlexW2002725390

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.