Format

Send to

Choose Destination
PLoS One. 2014 Feb 3;9(2):e87982. doi: 10.1371/journal.pone.0087982. eCollection 2014.

JMJD6 regulates ERα methylation on arginine.

Author information

1
Université de Lyon, F-69000 Lyon, France ; Université Lyon 1, F-69000 Lyon, France ; Inserm U1052, Centre de Recherche en Cancérologie de Lyon, F-69000 Lyon, France ; CNRS UMR5286, Centre de Recherche en Cancérologie de Lyon, F-69000 Lyon, France ; Equipe Labellisée « La Ligue »
2
Lebanese University, Faculty of Sciences, Doctoral School of Sciences and Technology, PRASE, Hadath, Lebanon.

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.

PMID:
24498420
PMCID:
PMC3912157
DOI:
10.1371/journal.pone.0087982
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for Public Library of Science Icon for PubMed Central
Loading ...
Support Center