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Submitted on May 6, 2003
Accepted on November 20, 2003
)
1 Department of Biosciences at Novum, Karolinska Institutet, S-14157, Huddinge, Sweden; Hormone Research Center, Chonnam National University, Gwangju 500-757, Republic of Korea.
* To whom correspondence should be addressed. 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 ERR
. All three isoforms share a high degree of amino acid identity especially in the DNA binding domain (DBD). ERR is a constitutively active transcriptional activator that regulates reporter elements driven by steroidogenic factor 1 (SF-1) response element (SF-1RE) and estrogen response element (ERE). However, it has the highest potency on a derivative of SF-1RE present in the small heterodimer partner (SHP) gene promoter called sft4 and unlike ERR and -, it fails to activate a palindromic thyroid hormone response element (TRE-pal). 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. Electrophoretic mobility shift (EMSA) and chromatin immunoprecipitation (ChIP) assays demonstrated that ERR binds to sft4, SF-1RE and TRE-pal 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 (RIP140) as a potent corepressor and peroxisome proliferator-activated receptor gamma (PPAR) coactivator 1 (PGC-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. Since ERR shows a similar tissue distribution as PGC-1 and RIP140, these two coregulators may act as key components of ERR mediated transcription.
•
sft4 •
SF-1RE •
TRE-pal •
RIP140 •
PGC-1
NURSA Molecule Pages Link:
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