Intermolecular interactions identify ligand-selective activity of estrogen receptor alpha/beta dimers.

ABSTRACT: Estrogen receptor (ER) dimerization is prerequisite for its activation of target gene transcription. Because the two forms of ER, ERalpha and ERbeta, exhibit opposing functions in cell proliferation, the ability of ligands to induce ERalpha/beta heterodimers vs. their respective homodimers is expected to have profound impacts on transcriptional outcomes and cellular growth. However, there is a lack of direct methods to monitor the formation of ERalpha/beta heterodimers in vivo and to distinguish the ability of estrogenic ligands to promote ER homo- vs. heterodimerization. Here, we describe bioluminescence resonance energy transfer (BRET) assays for monitoring the formation of ERalpha/beta heterodimers and their respective homodimers in live cells. We demonstrate that although both partners

SUBMITTER: Powell E 

PROVIDER: S-EPMC2596243 | biostudies-literature | 2008 Dec

REPOSITORIES: biostudies-literature