JMJD6 regulates ERα methylation on arginine.

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: Coralie Poulard, Juliette Rambaud, Nader Hussein, Laura Corbo, Muriel Le Romancer
Formato: article
Lenguaje:EN
Publicado: Public Library of Science (PLoS) 2014
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Acceso en línea:https://doaj.org/article/c93275f210f244afbb1176eb82b361df
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spelling oai:doaj.org-article:c93275f210f244afbb1176eb82b361df2021-11-18T08:34:06ZJMJD6 regulates ERα methylation on arginine.1932-620310.1371/journal.pone.0087982https://doaj.org/article/c93275f210f244afbb1176eb82b361df2014-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24498420/?tool=EBIhttps://doaj.org/toc/1932-6203ERα 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.Coralie PoulardJuliette RambaudNader HusseinLaura CorboMuriel Le RomancerPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 9, Iss 2, p e87982 (2014)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Coralie Poulard
Juliette Rambaud
Nader Hussein
Laura Corbo
Muriel Le Romancer
JMJD6 regulates ERα methylation on arginine.
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.
format article
author Coralie Poulard
Juliette Rambaud
Nader Hussein
Laura Corbo
Muriel Le Romancer
author_facet Coralie Poulard
Juliette Rambaud
Nader Hussein
Laura Corbo
Muriel Le Romancer
author_sort Coralie Poulard
title JMJD6 regulates ERα methylation on arginine.
title_short 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_sort jmjd6 regulates erα methylation on arginine.
publisher Public Library of Science (PLoS)
publishDate 2014
url https://doaj.org/article/c93275f210f244afbb1176eb82b361df
work_keys_str_mv AT coraliepoulard jmjd6regulateseramethylationonarginine
AT julietterambaud jmjd6regulateseramethylationonarginine
AT naderhussein jmjd6regulateseramethylationonarginine
AT lauracorbo jmjd6regulateseramethylationonarginine
AT murielleromancer jmjd6regulateseramethylationonarginine
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