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Submitted on August 24, 2004
Accepted on December 1, 2004
Laboratoire de génétique moléculaire, Institut de recherches cliniques de Montréal (IRCM), Montréal QC Canada H2W 1R7
* To whom correspondence should be addressed. E-mail: jacques.drouin{at}ircm.qc.ca.
Glucocorticoids (Gc) act through the Glucocorticoid Receptor (GR) to enhance or repress transcription of glucocorticoid responsive genes depending on the promoter and cellular context. Repression of POMC gene expression by Gc was proposed to use different mechanisms. We described the POMC promoter Nur response element (NurRE) as a target for Gc repression. NGFI-B (Nur77), an orphan nuclear receptor, and two related factors, Nurr1 and NOR1, bind the NurRE as homo- or heterodimers to enhance POMC gene expression in response to CRH. Gc antagonize CRH-stimulated as well as NGFI-B-dependent transcription. We now show that GR antagonizes NurRE-dependent transcription induced by all members of the Nur77 subfamily and that these nuclear receptors can all interact directly with GR. Transcriptional antagonism as well as direct protein:protein interaction between NGFI-B and GR take place primarily via their respective DNA binding domains, although DNA binding itself and the GR homodimerization interface are not involved. In vivo, GR and Nur factors can be co-immunoprecipitated while GR is recruited to the POMC promoter upon glucocorticoid action. Thus, our data suggest a mechanism for trans-repression between two nuclear receptors, GR and NGFI-B, that is unique, although quite similar to that proposed for trans-repression between GR and AP-1 or NF
B.
NURSA Molecule Pages Link:
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