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

doi:10.1091/mbc.E12-04-0267

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Article

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

Molecular biology of the cell - 1 Feb 2013

Carbonell Albert, Mazo Alexander, Serras Florenci, Corominas Montserrat

Abstract excerpt

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....

Topics

Animals
Drosophila Proteins
Drosophila melanogaster
Ecdysone
Enzyme Stability
Female
Genes, Lethal
Histone-Lysine N-Methyltransferase
Histones
Imaginal Discs
Larva

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Male

Methylation

Nuclear Proteins

Phenotype

Polytene Chromosomes

Protein Processing, Post-Translational

Protein Transport

Source

Open in PubMed Open full text

Identifiers

PMID: 23197473
DOI: 10.1091/mbc.E12-04-0267
PMCID: PMC3565548

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-23197473-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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Ash2 acts as an ecdysone receptor coactivator by stabilizing the histone methyltransferase Trr.PMID 23197473Read ↗

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