G9a-Mediated Methylation of ER Links the PHF20/MOF Histone Acetyltransferase Complex to Hormonal Gene Expression
Transcriptomics Dataset
FAIR Metrics
0 evaluations
General Information
| Accession | GSE76507 |
| Title | G9a-Mediated Methylation of ER Links the PHF20/MOF Histone Acetyltransferase Complex to Hormonal Gene Expression |
| Description | The euchromatin histone methyltransferase 2 (EHMT2, aka G9a) methylates histone H3K9 to repress gene expression, but it also acts as a coactivator for some nuclear receptors. The molecular mechanisms underlying this activation remain elusive. Here we show that G9a functions as a bona fide coactivator of the endogenous estrogen receptor (ER) in breast cancer cells in a histone methylation-independent manner. G9a dimethylates ER protein at lysine 235 both in vitro and in cells. Dimethylation of ERK235 (ERK235me2) is recognized by the Tudor domain of PHF20, which in turn recruits the MOF histone acetyltransferase (HAT) complex to ER target gene promoters to deposit histone H4K16 acetylation promoting active transcription. Together, our in vitro and in vivo data establish the molecular mechanism by which G9a functions as an ER coactivator. Along with the PHF20/MOF complex, G9a links the crosstalk between ER methylation and histone acetylation governing the epigenetic regulation of hormonal gene expression. |
| Landing Page | https://www.ncbi.nlm.nih.gov/geo/query/acc.cgi?acc=GSE76507 |
| Repository | Gene Expression Omnibus |
Tools
used to analyze the dataset
Canned Analyses
generated with the dataset
FAIR Evaluation
Sorry, you must be signed in to evaluate this object.
