Molecular Endocrinology, Vol 9, 243-254, Copyright © 1995 by Endocrine Society

ARTICLES

Two classes of proteins dependent on either the presence or absence of thyroid hormone for interaction with the thyroid hormone receptor

JW Lee, HS Choi, J Gyuris, R Brent and DD Moore
Department of Molecular Biology, Massachusetts General Hospital, Boston 02114, USA.

The thyroid hormone (T3) receptors (TRs) are hormone-dependent transcription factors that regulate expression of a variety of specific target genes. To help elucidate the mechanisms that underlie this transcriptional regulation and other potential TR activities, we used the yeast interaction trap to isolate clones encoding proteins that specifically interact with the ligand binding domain of the rat TR beta. Several such proteins, called Trips (TR-interacting proteins), were isolated from independent selections carried out either in the presence or absence of T3. Surprisingly, all of the Trips were dependent on hormone for interaction with the TR, with some interacting only when T3 is present and others only when it is absent. Nearly all of the Trips also show similar ligand-dependent interaction with the retinoid X receptor (RXR), but none interact with the glucocorticoid receptor under any conditions. The sequences of three of the Trips predict specific functional roles: one is an apparent human homolog of a yeast transcriptional coactivator, one is a new member of a class of nonhistone chromosomal proteins, and one contains a conserved domain associated with ubiquitination of specific target proteins. Consistent with the pleiotropic effects of TR and RXR, several other Trips show significant amino acid sequence similarity with proteins involved in various regulatory pathways. The inherent transcriptional activity of the Trips was tested in yeast, and a chimeric protein consisting of a fusion of Trip4 to the bacterial LexA repressor protein is a relatively strong transcriptional activator. Similar LexA fusions to Trip9 and Trip10 had no transcriptional activity on their own but, when coexpressed with both TR and RXR, conferred T3-dependent activation to a reporter gene controlled by LexA binding sites. We suggest that this indirect T3 response provides a novel mechanism for hormonal activation of gene expression, and that studies of the Trips will provide important insights into the specific mechanisms of action of TRs and other receptors.

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				W. Seol, B. Hanstein, M. Brown, and D. D. Moore Inhibition of Estrogen Receptor Action by the Orphan Receptor SHP (Short Heterodimer Partner) Mol. Endocrinol., October 1, 1998; 12(10): 1551 - 1557. [Abstract] [Full Text]

				Y. Liu, A. Takeshita, S. Misiti, W. W. Chin, and P. M. Yen Lack of Coactivator Interaction Can Be a Mechanism for Dominant Negative Activity by Mutant Thyroid Hormone Receptors Endocrinology, October 1, 1998; 139(10): 4197 - 4204. [Abstract] [Full Text] [PDF]

				A. Takeshita, P. M. Yen, M. Ikeda, G. R. Cardona, Y. Liu, N. Koibuchi, E. R. Norwitz, and W. W. Chin Thyroid Hormone Response Elements Differentially Modulate the Interactions of Thyroid Hormone Receptors with Two Receptor Binding Domains in the Steroid Receptor Coactivator-1 J. Biol. Chem., August 21, 1998; 273(34): 21554 - 21562. [Abstract] [Full Text] [PDF]

				S.-K. Lee, H.-S. Choi, M.-R. Song, M.-O. Lee, and J. W. Lee Estrogen Receptor, a Common Interaction Partner for a Subset of Nuclear Receptors Mol. Endocrinol., August 1, 1998; 12(8): 1184 - 1192. [Abstract] [Full Text]

				C.-X. Yuan, M. Ito, J. D. Fondell, Z.-Y. Fu, and R. G. Roeder The TRAP220 component of a thyroid hormone receptor- associated protein (TRAP) coactivator complex interacts directly with nuclear receptors in a ligand-dependent fashion PNAS, July 7, 1998; 95(14): 7939 - 7944. [Abstract] [Full Text] [PDF]

				H.-K. Lee, Y.-K. Lee, S.-H. Park, Y.-S. Kim, S. H. Park, J. W. Lee, H.-B. Kwon, J. Soh, D. D. Moore, and H.-S. Choi Structure and Expression of the Orphan Nuclear Receptor SHP Gene J. Biol. Chem., June 5, 1998; 273(23): 14398 - 14402. [Abstract] [Full Text] [PDF]

				M. H. Glickman, D. M. Rubin, V. A. Fried, and D. Finley The Regulatory Particle of the Saccharomyces cerevisiae Proteasome Mol. Cell. Biol., June 1, 1998; 18(6): 3149 - 3162. [Abstract] [Full Text]

				E. Treuter, T. Albrektsen, L. Johansson, J. Leers, and J.-A. Gustafsson A Regulatory Role for RIP140 in Nuclear Receptor Activation Mol. Endocrinol., June 1, 1998; 12(6): 864 - 881. [Abstract] [Full Text]

				F. Hirano, M. Chung, H. Tanaka, N. Maruyama, I. Makino, D. D. Moore, and C. Scheidereit Alternative Splicing Variants of Ikappa Bbeta Establish Differential NF-kappa B Signal Responsiveness in Human Cells Mol. Cell. Biol., May 1, 1998; 18(5): 2596 - 2607. [Abstract] [Full Text]

				S.-Y. Na, S.-K. Lee, S.-J. Han, H.-S. Choi, S.-Y. Im, and J. W. Lee Steroid Receptor Coactivator-1 Interacts with the p50 Subunit and Coactivates Nuclear Factor kappa B-mediated Transactivations J. Biol. Chem., May 1, 1998; 273(18): 10831 - 10834. [Abstract] [Full Text] [PDF]

				R. M. Lavinsky, K. Jepsen, T. Heinzel, J. Torchia, T.-M. Mullen, R. Schiff, A. L. Del-Rio, M. Ricote, S. Ngo, J. Gemsch, et al. Diverse signaling pathways modulate nuclear receptor recruitment of N-CoR and SMRT complexes PNAS, March 17, 1998; 95(6): 2920 - 2925. [Abstract] [Full Text] [PDF]

				S.-Y. Na, H.-J. Kim, S.-K. Lee, H.-S. Choi, D.-S. Na, M.-O. Lee, M. Chung, D. D. Moore, and J. W. Lee Ikappa Bbeta Interacts with the Retinoid X Receptor and Inhibits Retinoid-dependent Transactivation in Lipopolysaccharide-treated Cells J. Biol. Chem., February 6, 1998; 273(6): 3212 - 3215. [Abstract] [Full Text] [PDF]

				T. Tagami and J. L. Jameson Nuclear Corepressors Enhance the Dominant Negative Activity of Mutant Receptors That Cause Resistance to Thyroid Hormone Endocrinology, February 1, 1998; 139(2): 640 - 650. [Abstract] [Full Text] [PDF]

				D. C. Thurmond and A. G. Goodridge Characterization of Thyroid Hormone Response Elements in the Gene for Chicken Malic Enzyme. FACTORS THAT INFLUENCE TRIIODOTHYRONINE RESPONSIVENESS J. Biol. Chem., January 16, 1998; 273(3): 1613 - 1622. [Abstract] [Full Text] [PDF]

				P Tate, M Lee, S Tweedie, W. Skarnes, and W. Bickmore Capturing novel mouse genes encoding chromosomal and other nuclear proteins J. Cell Sci., January 9, 1998; 111(17): 2575 - 2585. [Abstract] [PDF]

				Y. Liu, A. Takeshita, T. Nagaya, A. Baniahmad, W. W. Chin, and P. M. Yen An Inhibitory Region of the DNA-Binding Domain of Thyroid Hormone Receptor Blocks Hormone-Dependent Transactivation Mol. Endocrinol., January 1, 1998; 12(1): 34 - 44. [Abstract] [Full Text]

				R. K. Gill, L. M. Atkins, B. W. Hollis, and N. H. Bell Mapping the Domains of the Interaction of the Vitamin D Receptor and Steroid Receptor Coactivator-1 Mol. Endocrinol., January 1, 1998; 12(1): 57 - 65. [Abstract] [Full Text]

				A. Abe, N. Emi, M. Tanimoto, H. Terasaki, T. Marunouchi, and H. Saito Fusion of the Platelet-Derived Growth Factor Receptor beta  to a Novel Gene CEV14 in Acute Myelogenous Leukemia After Clonal Evolution Blood, December 1, 1997; 90(11): 4271 - 4277. [Abstract] [Full Text] [PDF]

				T. Monden, F. E. Wondisford, and A. N. Hollenberg Isolation and Characterization of a Novel Ligand-dependent Thyroid Hormone Receptor-coactivating Protein J. Biol. Chem., November 21, 1997; 272(47): 29834 - 29841. [Abstract] [Full Text] [PDF]

				W. Porter, B. Saville, D. Hoivik, and S. Safe Functional Synergy between the Transcription Factor Sp1 and the Estrogen Receptor Mol. Endocrinol., October 1, 1997; 11(11): 1569 - 1580. [Abstract] [Full Text]

				T. A. McKinsey, Z.-L. Chu, and D. W. Ballard Phosphorylation of the PEST Domain of Ikappa Bbeta Regulates the Function of NF-kappa B/Ikappa Bbeta Complexes J. Biol. Chem., September 5, 1997; 272(36): 22377 - 22380. [Abstract] [Full Text] [PDF]

				K.-H. Chang, Y. Chen, T.-T. Chen, W.-H. Chou, P.-L. Chen, Y.-Y. Ma, T. L. Yang-Feng, X. Leng, M.-J. Tsai, B. W. O'Malley, et al. A thyroid hormone receptor coactivator negatively regulated by the retinoblastoma protein PNAS, August 19, 1997; 94(17): 9040 - 9045. [Abstract] [Full Text] [PDF]

				F. M. Chuang, B. L. West, J. D. Baxter, and F. Schaufele Activities in Pit-1 Determine Whether Receptor Interacting Protein 140 Activates or Inhibits Pit-1/Nuclear Receptor Transcriptional Synergy Mol. Endocrinol., August 1, 1997; 11(9): 1332 - 1341. [Abstract] [Full Text]