JMJD6 Regulates ERα Methylation on Arginine

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 wit...

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Autores principales: Poulard, Coralie, Rambaud, Juliette, Hussein, Nader, Corbo, Laura, Le Romancer, Muriel
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2014
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3912157/
https://www.ncbi.nlm.nih.gov/pubmed/24498420
http://dx.doi.org/10.1371/journal.pone.0087982
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author Poulard, Coralie
Rambaud, Juliette
Hussein, Nader
Corbo, Laura
Le Romancer, Muriel
author_facet Poulard, Coralie
Rambaud, Juliette
Hussein, Nader
Corbo, Laura
Le Romancer, Muriel
author_sort Poulard, Coralie
collection PubMed
description 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.
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spelling pubmed-39121572014-02-04 JMJD6 Regulates ERα Methylation on Arginine Poulard, Coralie Rambaud, Juliette Hussein, Nader Corbo, Laura Le Romancer, Muriel PLoS One Research Article 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. Public Library of Science 2014-02-03 /pmc/articles/PMC3912157/ /pubmed/24498420 http://dx.doi.org/10.1371/journal.pone.0087982 Text en © 2014 Poulard et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Poulard, Coralie
Rambaud, Juliette
Hussein, Nader
Corbo, Laura
Le Romancer, Muriel
JMJD6 Regulates ERα Methylation on Arginine
title JMJD6 Regulates ERα Methylation on Arginine
title_full JMJD6 Regulates ERα Methylation on Arginine
title_fullStr JMJD6 Regulates ERα Methylation on Arginine
title_full_unstemmed JMJD6 Regulates ERα Methylation on Arginine
title_short JMJD6 Regulates ERα Methylation on Arginine
title_sort jmjd6 regulates erα methylation on arginine
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3912157/
https://www.ncbi.nlm.nih.gov/pubmed/24498420
http://dx.doi.org/10.1371/journal.pone.0087982
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