Please use this identifier to cite or link to this item: http://hdl.handle.net/2445/34233
Title: Ash2 acts as an Ecdysone Receptor coactivator by stabilizing the histone methyltransferase Trr.
Author: Carbonell Sanroma, Albert
Mazo, A.
Serras Rigalt, Florenci
Corominas, Montserrat (Corominas Guiu)
Keywords: Expressió gènica
Regulació genètica
Mutació (Biologia)
Gene expression
Genetic regulation
Mutation (Biology)
Issue Date: 1-Feb-2013
Publisher: American Society for Cell Biology
Abstract: 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.
Note: Reproducció del document publicat a: http://dx.doi.org/10.1091/mbc.E12-04-0267
It is part of: Molecular Biology of the Cell, 2013, vol. 24, num. 3, p. 361-372
Related resource: http://dx.doi.org/10.1091/mbc.E12-04-0267
URI: http://hdl.handle.net/2445/34233
ISSN: 1059-1524
Appears in Collections:Articles publicats en revistes (Genètica, Microbiologia i Estadística)

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