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Volume 272, Number 20, Issue of May 16, 1997 pp. 13060-13065
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Thyroid Hormone-mediated Enhancement of Heterodimer Formation between Thyroid Hormone Receptor beta  and Retinoid X Receptor

(Received for publication, December 18, 1996, and in revised form, March 5, 1997)

Trevor N. Collingwood Dagger , Alison Butler , Yukiko Tone Dagger , Rory J. Clifton-Bligh Dagger , Malcolm G. Parker and V. Krishna K. Chatterjee Dagger

From the Dagger  Department of Medicine, University of Cambridge, Addenbrooke's Hospital, Cambridge CB2 2QQ and the  Molecular Endocrinology Laboratory, Imperial Cancer Research Fund, Lincoln's Inn Fields, London WC2A 3PX, United Kingdom

A subset of nuclear receptors, including those for thyroid hormone (TR), retinoic acid, vitamin D3, and eicosanoids, can form heterodimers with the retinoid X receptor (RXR) on DNA regulatory elements in the absence of their cognate ligands. In a mammalian two-hybrid assay, we have found that recruitment of a VP16-RXR chimera by a Gal4-TRbeta ligand-binding domain fusion is enhanced up to 50-fold by thyroid hormone (T3). This was also observed with a mutant fusion, Gal4-TR(L454A), lacking ligand-inducible activation function (AF-2) and unable to interact with putative coactivators, suggesting that the AF-2 activity of TR or intermediary cofactors is not involved in this effect. The wild-type and mutant Gal4-TR fusions also exhibited hormone-dependent recruitment of RXR in yeast. Hormone-dependent recruitment of RXR was also evident with another Gal4-TR mutant, AHTm, which does not interact with the nuclear receptor corepressor N-CoR, suggesting that ligand-enhanced dimerization is not a result of T3-induced corepressor release. Finally, we have shown that the interaction between RXR and TR is augmented by T3 in vitro, arguing against altered expression of either partner in vivo mediating this effect. We propose that ligand-dependent heterodimerization of TR and RXR in solution may provide a further level of control in nuclear receptor signaling.


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