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Department of Biosciences at Novum, Karolinska Institutet (S.S., J.M., D.B., E.T., J.-A.G.), S-14157 Huddinge, Sweden; Hormone Research Center (H.-J.K., H.-S.C.), Chonnam National University, Gwangju 500-757, Republic of Korea
Address all correspondence and requests for reprints to: Sabyasachi Sanyal, Ph.D., Department of Biosciences at Novum, Karolinska Institutet, S-14157 Huddinge, Sweden. E-mail: sabyasachi.sanyal{at}cbt.ki.se.
The estrogen receptor-related receptor 
(ERR/ERR3/NR3B3) is the newest member of the ERR subfamily that also includes ERR
and ERRß. All three isoforms share a high degree of amino acid identity especially in the DNA binding domain. ERR is a constitutively active transcriptional activator that regulates reporter elements driven by steroidogenic factor 1 response element (SF-1RE) and estrogen response element. However, it has the highest potency on a derivative of SF-1RE present in the small heterodimer partner gene promoter called sft4 and unlike ERR and -ß, it fails to activate a palindromic thyroid hormone response element. To investigate the mechanism behind this response element-specific differential transcriptional activity of ERR, the interactions of ERR and the aforementioned response elements was monitored. EMSA and chromatin immunoprecipitation assays demonstrated that ERR binds to sft4, SF-1RE, and palindromic thyroid hormone response element albeit with different degrees of affinity, but causes hyperacetylation of sft4 and SF-1RE templates only. Limited proteolysis assays showed that ERR, bound to different elements, shows differential trypsin sensitivity. A search for novel coregulators of ERR led to the identification of receptor interacting protein 140 as a potent corepressor and peroxisome proliferator-activated receptor coactivator 1 as a potent coactivator of ERR. DNA-dependent pull-down and transient transfection assays demonstrated that, on different DNA elements, ERR exhibits differential cofactor interactions, which in turn dictate its transcriptional activity. Because ERR shows a similar tissue distribution as peroxisome proliferator-activated receptor coactivator 1 and receptor interacting protein 140, these two coregulators may act as key components of ERR-mediated transcription.
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