Abstract
To understand the mechanism by which estrogen receptor (ER) activates transcription in a tissue specific fashion, we isolated ERα binding protein (ERBP) by performing yeast two-hybrid screening with human mammary gland cDNA library. ERBP is a nuclear protein and its mRNA is ubiquitously expressed. The in vitro interaction of ERBP with ERα was demonstrated by GST pull-down assay and this interaction was enhanced by estrogen. In addition, ERBP also bound to PPARγ, RXRα, and ERβ. ERBP interacted with the DNA binding domain and the hinge region of ERα. There are two ERα binding regions on ERBP. The binding of ERBP region at C-terminus to ERα is increased by estrogen while the binding of ERBP region at N-terminus is not affected by estrogen. The interaction of ERBP with ERα was further confirmed in vivo by immunoprecipitation. Transient transfection experiment demonstrated that ERBP enhanced the transcriptional activity of ERα.
Original language | English (US) |
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Pages (from-to) | 54-59 |
Number of pages | 6 |
Journal | Biochemical and Biophysical Research Communications |
Volume | 317 |
Issue number | 1 |
DOIs | |
State | Published - Apr 23 2004 |
Funding
We thank Dr. Janardan K. Reddy for his support and comments on the manuscript. This work was supported by National Institutes of Health Grant K08 ES 00356 and CA 88898 (Y.J.Z), CA 84472 (M.S.R.), and DOD Breast Cancer Research Program (Y.J.Z).
Keywords
- Coactivator
- Estrogen receptor binding protein
- Estrogen receptor α
ASJC Scopus subject areas
- Molecular Biology
- Biophysics
- Biochemistry
- Cell Biology