FB2025_01 , released February 20, 2025
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Citation
Carbonell, A., Mazo, A., Serras, F., Corominas, M. (2013). Ash2 acts as an ecdysone receptor coactivator by stabilizing the histone methyltransferase Trr.  Mol. Biol. Cell 24(3): 361--372.
FlyBase ID
FBrf0222162
Publication Type
Research paper
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.
PubMed ID
PubMed Central ID
PMC3565548 (PMC) (EuropePMC)
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Secondary IDs
    Language of Publication
    English
    Additional Languages of Abstract
    Parent Publication
    Publication Type
    Journal
    Abbreviation
    Mol. Biol. Cell
    Title
    Molecular Biology of the Cell
    Publication Year
    1992-
    ISBN/ISSN
    1059-1524
    Data From Reference
    Genes (6)
    Physical Interactions (1)