The Orphan Nuclear Receptor SHP Inhibits Hepatocyte Nuclear Factor 4 and Retinoid X Receptor Transactivation: Two Mechanisms for Repression

doi:10.1128/MCB.20.1.187-195.2000

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Molecular and Cellular Biology, January 2000, p. 187-195, Vol. 20, No. 1
0270-7306/0/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

The Orphan Nuclear Receptor SHP Inhibits Hepatocyte Nuclear Factor 4 and Retinoid X Receptor Transactivation: Two Mechanisms for Repression

Yoon-Kwang Lee,¹ Helen Dell,² Dennis H. Dowhan,¹ Margarita Hadzopoulou-Cladaras,² and David D. Moore¹^,^*

Department of Molecular and Cellular Biology, Baylor College of Medicine, Houston, Texas 77030,¹ and Department of Medicine, Section of Molecular Genetics, Cardiovascular Institute, Boston University School of Medicine, Center for Advanced Biomedical Research, Boston, Massachusetts 02118²

Received 26 July 1999/Returned for modification 25 August 1999/Accepted 27 September 1999

The orphan nuclear hormone receptor SHP interacts with a number of other nuclear hormone receptors and inhibits their transcriptionalactivity. Several mechanisms have been suggested to account forthis inhibition. Here we show that SHP inhibits transactivationby the orphan receptor hepatocyte nuclear factor 4 (HNF-4) andthe retinoid X receptor (RXR) by at least two mechanisms. SHPinteracts with the same HNF-4 surface recognized by transcriptionalcoactivators and competes with them for binding in vivo. The minimalSHP sequences previously found to be required for interactionwith other receptors are sufficient for interaction with HNF-4,although deletion results indicate that additional C-terminalsequences are necessary for full binding and coactivator competition.These additional sequences include those associated with directtranscriptional repressor activity of SHP. SHP also competes withcoactivators for binding to ligand-activated RXR, and based onthe ligand-dependent interaction with other nuclear receptors,it is likely that coactivator competition is a general featureof SHP-mediated repression. The minimal receptor interaction domainof SHP is sufficient for full interaction with RXR, as previouslydescribed. This domain is also sufficient for full coactivatorcompetition. Functionally, however, full inhibition of RXR transactivationrequires the presence of the C-terminal repressor domain, withonly weak inhibition associated with this receptor interactiondomain. Overall, these results suggest that SHP represses nuclearhormone receptor-mediated transactivation via two separate steps:first by competition with coactivators and then by direct effectsof its transcriptional repressorfunction.

^* Corresponding author. Mailing address: Department of Molecular and Cellular Biology, Baylor College of Medicine, One BaylorPlaza, Houston, TX 77030. Phone: (713) 798-3313. Fax: (713) 798-3017.E-mail: moore{at}bcm.tmc.edu.

Molecular and Cellular Biology, January 2000, p. 187-195, Vol. 20, No. 1
0270-7306/0/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

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