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Endocrine-Related Cancer 16 (2) 319 -323     DOI: 10.1677/ERC-08-0305
Copyright © 2009 by the Society for Endocrinology
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Epigenetics meets estrogen receptor: regulation of estrogen receptor by direct lysine methylation

 Qun Zhou1, Patrick G Shaw2,3 and Nancy E Davidson2,3

1 Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, Baltimore, Maryland 21201, USA
2 Department of Biochemistry and Molecular Biology, Johns Hopkins Bloomberg School of Public Health, Baltimore, Maryland 21205, USA
3 University of Pittsburgh Cancer Institute, UPMC Cancer Pavilion, 5150 Centre Avenue Suite 500, Pittsburgh, Pennsylvania 15232, USA

(Correspondence should be addressed to N E Davidson; Email: davidsonne{at}upmc.edu)

The nuclear hormone receptor estrogen receptor {alpha} (ER{alpha}) promotes cellular growth through ligand-dependent activation of specific target genes, a process which is targeted in the treatment of ER{alpha}-expressing breast cancers. ER{alpha} activity is regulated at the protein level by post-translational modifications including phosphorylation and acetylation. A study now shows that ER{alpha} can also be directly methylated at lysine 302 (K302) by SET7, a histone methyltransferase that is known to monomethylate H3K4 and is associated with transcriptional activation. It was shown that K302 methylation stabilizes ER{alpha} protein and is suggested to increase sensitivity of ER{alpha} to estrogens, enhancing transcription of estrogen response elements. 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 into the complex regulation of ER{alpha} stability and ligand sensitivity.






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