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Papers In Press, published online ahead of print March 12, 2002
Department of Biochemistry, University of Kuopio, Kuopio
Corresponding Author: carlberg{at}messi.uku.fi
Nuclear receptors and POU domain factors form two important transcription factor families, for which several levels of functional interference have been described. In this study, the adopted orphan receptors constitutive androstane receptor (CAR) and pregnane X receptor (PXR) were found to perform direct protein-protein interactions with Pit-1, a representative POU domain factor. The ligand-dependent interaction profile of Pit-1 with CAR, PXR and the vitamin D receptor (VDR) in solution showed to be that of a corepressor. In the absence of receptor agonist Pit-1 inhibited the complex formation of nuclear receptors with the retinoid X receptor (RXR) on DNA. Also in living cells, Pit-1 and Oct-1, another POU domain factor, behaved like corepressors of nuclear receptor signaling and Pit-1-mediated repression involves histone deacetylases (HDACs). Conversely, VDR, CAR and PXR were shown to act as repressors of Pit-1 signaling in different cell lines (MCF-7, HaCaT and GH4C1). This repression was found to be independent of HDACs and seems to be based on a competition of nuclear receptors with coactivator and corepressor proteins for overlaying interaction interfaces on the surface of Pit-1. Taken together, this study suggests that crossrepression should occur in all tissues, in which POU domain factors and non-liganded nuclear receptors meet each other.
J. Biol. Chem, 10.1074/jbc.M200205200
Submitted on January 8, 2002
Revised on February 11, 2002
Accepted on March 12, 2002
Crossrepression: A functional consequence of the physical interaction of non-liganded nuclear receptors and POU domain transcription factors
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