JMJD6 Regulates ERα Methylation on Arginine
Author(s) -
Coralie Poulard,
Juliette Rambaud,
Nader Hussein,
Laura Corbo,
Muriel Le Romancer
Publication year - 2014
Publication title -
plos one
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.99
H-Index - 332
ISSN - 1932-6203
DOI - 10.1371/journal.pone.0087982
Subject(s) - demethylase , demethylation , methylation , arginine , microbiology and biotechnology , gene silencing , regulator , function (biology) , chemistry , dna methylation , biology , biochemistry , epigenetics , gene expression , amino acid , gene
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.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom