Abstract
ERα functions are tightly controlled by numerous post-translational modifications including arginine methylation, which is required to mediate the extranuclear functions of the receptor. We report that upon oestrogenic stimulation, JMJD6, the only arginine demethylase described so far, interacts with and regulates methylated ERα (metERα) function. Moreover, by combining the silencing of JMJD6 with demethylation assays, we show that metERα is a new substrate for JMJD6. We propose that the demethylase activity of JMJD6 is a decisive regulator of the rapid physiological responses to oestrogen.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Arginine / chemistry*
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Blotting, Western
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Breast Neoplasms / genetics*
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Breast Neoplasms / metabolism
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Chromatography, Affinity
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DNA Methylation*
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Estrogen Receptor alpha / genetics*
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Estrogen Receptor alpha / metabolism
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Female
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Gene Expression Regulation, Neoplastic*
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Humans
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Image Processing, Computer-Assisted
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Immunoprecipitation
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Jumonji Domain-Containing Histone Demethylases / genetics
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Jumonji Domain-Containing Histone Demethylases / metabolism*
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Protein Processing, Post-Translational*
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Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
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Tumor Cells, Cultured
Substances
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ESR1 protein, human
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Estrogen Receptor alpha
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Arginine
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JMJD6 protein, human
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Jumonji Domain-Containing Histone Demethylases
Grants and funding
Funding for this study was provided by: Fondation Arc Cancer, Ligue Nationale Contre le Cancer, Fondation de France, and Ministère de la Recherche. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.