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Accepted Preprint first posted online on 10 February 2009

Endocrine-Related Cancer 2009;16:319.

DOI: 10.1677/ERC-08-0305
Copyright © 2009 by the Society for Endocrinology.
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COMMENTARY

Epigenetics meets estrogen receptor: regulation of estrogen receptor by direct lysine methylation

 Qun Zhou, Patrick Shaw and Nancy Davidson

Q Zhou, Biochemistry and Molecular Biology, University of Maryland, Baltimore, United States
P Shaw, Biochemistry and Molecular Biology, Johns Hopkins Bloomberg School of Public Health, Baltimore, United States
N Davidson, Oncology, University of Pittsburgh Cancer Institute, Pittsburgh, United States

Correspondence: Patrick Shaw, Email: pshaw{at}jhsph.edu

Abstract

The nuclear hormone receptor estrogen receptor alpha (ERalpha) promotes cellular growth through ligand dependent activation of specific target genes, a process which is targeted in the treatment of ERalpha-expressing breast cancers. ERalpha activity is regulated at the protein level by posttranslational modifications (PTMs) including phosphorylation and acetylation. A study now shows that ERalpha can also be directly methylated at lysine 302 (K302) by SET7, a histone methyltransferase (HMT), which is known to monomethylate H3K4 and is associated with transcriptional activation. It was shown that K302 methylation stabilizes ERalpha protein and is suggested to increase sensitivity of ERalpha to estrogens, enhancing transcription of Estrogen Response Elements (ERE). Furthermore, SET7 methylation of K302 is enhanced by a breast cancer-associated mutation at K303 (K303R) in vitro. These findings provide an additional mechanism of SET7 mediated transcriptional activation as well as potential insight to the complex regulation of ERalpha stability and ligand sensitivity.






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