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J Biol Chem, Vol. 275, Issue 3, 1787-1792, January 21, 2000

Thyroid Hormone-independent Interaction between the Thyroid Hormone Receptor beta 2 Amino Terminus and Coactivators*

Corinna Oberste-BerghausDagger , Kerstin ZangerDagger , Koshi Hashimoto, Ronald N. Cohen, Anthony N. Hollenberg, and Fredric E. Wondisford*

From the Thyroid Unit, Beth Israel Deaconess Medical Center and Harvard Medical School, Boston, Massachusetts 02215

Thyroid hormone receptors (TRs) mediate hormone action by binding to DNA response elements (TREs) and either activating or repressing gene expression in the presence of ligand, T3. Coactivator recruitment to the AF-2 region of TR in the presence of T3 is central to this process. The different TR isoforms, TR-beta 1, TR-beta 2, and TR-alpha 1, share strong homology in their DNA- and ligand-binding domains but differ in their amino-terminal domains. Because TR-beta 2 exhibits greater T3-independent activation on TREs than other TR isoforms, we wanted to determine whether coactivators bound to TR-beta 2 in the absence of ligand. Our results show that TR-beta 2, unlike TR-beta 1 or TR-alpha 1, is able to bind certain coactivators (CBP, SRC-1, and pCIP) in the absence of T3 through a domain which maps to the amino-terminal half of its A/B domain. This interaction is specific for certain coactivators, as TR-beta 2 does not interact with other co-factors (p120 or the CBP-associated factor (pCAF)) in the absence of T3. The minimal TR-beta 2 domain for coactivator binding is aa 21-50, although aa 1-50 are required for the full functional response. Thus, isoform-specific regulation by TRs may involve T3-independent coactivator recruitment to the transcription complex via the AF-1 domain.

* This work was supported by grants from the National Institute of Health (to R. N. C., A. N. H., and F. E. W.) and by a research grant of the Deutschen Akademischen Austauschdienst (to C. O. B.).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 These authors contributed equally to the study.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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