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Originally published In Press as doi:10.1074/jbc.M200205200 on March 12, 2002

J. Biol. Chem., Vol. 277, Issue 21, 18501-18509, May 24, 2002
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Cross-repression, a Functional Consequence of the Physical Interaction of Non-liganded Nuclear Receptors and POU Domain Transcription Factors*

Manuel Macias Gonzalez and Carsten CarlbergDagger

From the Department of Biochemistry, University of Kuopio, FIN-70211 Kuopio, Finland

Nuclear receptors (NRs) 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 in solution was shown to be that of a corepressor. In the absence of receptor agonist Pit-1 inhibited the complex formation of NRs with the retinoid X receptor on DNA. Also in living cells, Pit-1 and Oct-1, another POU domain factor, behaved like corepressors of NR signaling, and Pit-1-mediated repression was found to involve histone deacetylases. Conversely vitamin D receptor, 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 histone deacetylases and seems to be based on a competition of NRs with coactivator and corepressor proteins for overlaying interaction interfaces on the surface of Pit-1. Taken together this study suggests that cross-repression should occur in all tissues in which POU domain factors and non-liganded NRs meet each other.

* This work was supported by Academy of Finland Grants 50319 and 50331 (to C. C.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed: Dept. of Biochemistry, University of Kuopio, P.O. box 1627, FIN-70211 Kuopio, Finland. Tel.: 358-17-163062; Fax: 358-17-2811510; E-mail: carlberg@messi. uku.fi.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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