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Please use this identifier to cite or link to this item: https://hdl.handle.net/2445/34233
Ash2 acts as an Ecdysone Receptor coactivator by stabilizing the histone methyltransferase Trr.
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The molting hormone ecdysone triggers chromatin changes via histone modifica- tions 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 tran- scriptional 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 ecdy- sone-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 re- quired for its stabilization. Thus we propose that Ash2 functions together with Trr as an ecdysone receptor coactivator.
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CARBONELL SANROMA, Albert, et al. Ash2 acts as an Ecdysone Receptor coactivator by stabilizing the histone methyltransferase Trr. Molecular Biology of the Cell. 2013. Vol. 24, num. 3, pags. 361-372. ISSN 1059-1524. [consulted: 6 of June of 2026]. Available at: https://hdl.handle.net/2445/34233