| Literature DB >> 20448663 |
Sujit S Nair1, Binoj C Nair, Valerie Cortez, Dimple Chakravarty, Eric Metzger, Roland Schüle, Darrell W Brann, Rajeshwar R Tekmal, Ratna K Vadlamudi.
Abstract
Histone methylation has a key role in oestrogen receptor (ERalpha)-mediated transactivation of genes. Proline glutamic acid and leucine-rich protein 1 (PELP1) is a new proto-oncogene that functions as an ERalpha co-regulator. In this study, we identified histone lysine demethylase, KDM1, as a new PELP1-interacting protein. These proteins, PELP1 and KDM1, were both recruited to ERalpha target genes, and PELP1 depletion affected the dimethyl histone modifications at ERalpha target genes. Dimethyl-modified histones H3K4 and H3K9 are recognized by PELP1, and PELP1 alters the substrate specificity of KDM1 from H3K4 to H3K9. Effective demethylation of dimethyl H3K9 by KDM1 requires a KDM1-ERalpha-PELP1 functional complex. These results suggest that PELP1 is a reader of H3 methylation marks and has a crucial role in modulating the histone code at the ERalpha target genes.Entities:
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Year: 2010 PMID: 20448663 PMCID: PMC2892318 DOI: 10.1038/embor.2010.62
Source DB: PubMed Journal: EMBO Rep ISSN: 1469-221X Impact factor: 8.807