Gene regulation by thyroid hormone

Trends in Endocrinology and Metabolism

Volumn 11, Issue 6, 2000, Pages 207-211

  Wu, Yifei ^a   Koenig, Ronald J ^a  

^a UNIVERSITY OF MICHIGAN HEALTH SYSTEM   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE DEACETYLASE; LIGAND; LIOTHYRONINE; THYROID HORMONE; THYROID HORMONE RECEPTOR; THYROXINE;

ACETYLATION; CHROMATIN STRUCTURE; CONFORMATIONAL TRANSITION; DEACETYLATION; DIMERIZATION; DNA SEQUENCE; DNA TRANSCRIPTION; DOWN REGULATION; ENZYME ACTIVITY; GENE ACTIVATION; GENE CONTROL; GENE REPRESSION; GENETIC TRANSCRIPTION; HORMONAL REGULATION; HORMONE ACTION; HORMONE RECEPTOR INTERACTION; HUMAN; LIGAND BINDING; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; RECEPTOR UPREGULATION; REVIEW; RUBINSTEIN SYNDROME;

ANIMALS; GENE EXPRESSION REGULATION; HUMANS; RECEPTORS, THYROID HORMONE; THYROID HORMONES;

EID: 0033853497     PISSN: 10432760     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1043-2760(00)00263-0     Document Type: Review

References (45)

1. Mangelsdorf D.J.et al. The nuclear receptor superfamily: the second decade. Cell. 83:1995;835-839.
2. Refetoff S.et al. The syndromes of resistance to thyroid hormone. Endocr. Rev. 14:1993;348-399.
3. Forrest D.et al. Recessive resistance to thyroid hormone in mice lacking thyroid hormone receptor beta: evidence for tissue-specific modulation of receptor function. EMBO J. 15:1996;3006-3015.
4. Gauthier K.et al. Different functions for the thyroid hormone receptors TRalpha and TRbeta in the control of thyroid hormone production and post-natal development. EMBO J. 18:1999;623-631.
5. Wikström L.et al. Abnormal heart rate and body temperature in mice lacking thyroid hormone receptor alpha1. EMBO J. 17:1998;455-461.
6. Barettino D.et al. Characterization of the ligand-dependent transactivation domain of thyroid hormone receptor. EMBO J. 13:1994;3039-3049.
7. Wurtz J.-M.et al. A canonical structure for the ligand-binding domain of nuclear receptors. Nat. Struct. Biol. 3:1996;87-94.
8. Wagner R.L.et al. A structural role for hormone in the thyroid hormone receptor. Nature. 378:1995;690-697.
9. Oñate S.A.et al. Sequence and characterization of a coactivator for the steroid hormone receptor superfamily. Science. 270:1995;1354-1357.
10. Voegel J.J.et al. TIF2, a 160 kDa transcriptional mediator for the ligand-dependent activation function AF-2 of nuclear receptors. EMBO J. 15:1996;3667-3675.
11. Torchia J.et al. The transcriptional co-activator p/CIP binds CBP and mediates nuclear-receptor function. Nature. 387:1997;677-684.
12. Chakravarti D.et al. Role of CBP/P300 in nuclear receptor signalling. Nature. 383:1996;99-103.
13. Blanco J.C.G.et al. PCAF is a nuclear receptor coactivator. Genes Dev. 12:1998;1638-1651.
14. Fondell J.D.et al. Ligand induction of a transcriptionally active thyroid hormone receptor coactivator complex. Proc. Natl. Acad. Sci. U. S. A. 93:1996;8329-8333.
15. Heery D.M.et al. A signature motif in transcriptional co-activators mediates binding to nuclear receptor. Nature. 387:1997;733-736.
16. McInerney E.M.et al. Determinants of coactivator LXXLL motif specificity in nuclear receptor transcriptional activation. Genes Dev. 12:1998;3357-3368.
17. Westin S.et al. Interactions controlling the assembly of nuclear-receptor heterodimers and co-activators. Nature. 395:1998;199-202.
18. Nolte R.T.et al. Ligand binding and co-activator assembly of the peroxisome proliferator-activated receptor-gamma. Nature. 395:1998;137-143.
19. Xu J.et al. Partial hormone resistance in mice with disruption of the steroid receptor coactivator-1 (SRC-1) gene. Science. 279:1998;1922-1925.
20. Weiss R.E.et al. Mice deficient in the steroid receptor co-activator 1 (SRC-1) are resistant to thyroid hormone. EMBO J. 18:1999;1900-1904.
21. Ogryzko V.V.et al. The transcriptional coactivators p300 and CBP are histone acetyltransferases. Cell. 87:1996;953-959.
22. Spencer T.E.et al. Steroid receptor coactivator-1 is a histone acetyltransferase. Nature. 389:1997;194-198.
23. Wong J.M.et al. Distinct requirements for chromatin assembly in transcriptional repression by thyroid hormone receptor and histone deacetylase. EMBO J. 17:1998;520-534.
24. Li Q.et al. p300 stimulates transcription instigated by ligand-bound thyroid hormone receptor at a step subsequent to chromatin disruption. EMBO J. 18:1999;5634-5652.
25. Gu W., Roeder R.G. Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain. Cell. 90:1997;595-606.
26. Kim M.K.et al. In vivo transcription factor recruitment during thyroid hormone receptor-mediated activation. Proc. Natl. Acad. Sci. U. S. A. 96:1999;10092-10097.
27. Olson D.P., Koenig R.J. Thyroid function in Rubinstein-Taybi syndrome. J. Clin. Endocrinol. Metab. 82:1997;3264-3266.
28. Rachez C.et al. Ligand-dependent transcription activation by nuclear receptors requires the DRIP complex. Nature. 398:1999;824-828.
29. Näär A.M.et al. Composite co-activator ARC mediates chromatin-directed transcriptional activation. Nature. 398:1999;828-832.
30. Yuan C.X.et al. The TRAP220 component of a thyroid hormone receptor-associated protein (TRAP) coactivator complex interacts directly with nuclear receptors in a ligand-dependent fashion. Proc. Natl. Acad. Sci. U. S. A. 95:1998;7939-7944.
31. Treuter E.et al. Competition between thyroid hormone receptor-associated protein (TRAP) 220 and transcriptional intermediary factor (TIF) 2 for binding to nuclear receptors - implications for the recruitment of TRAP and P160 coactivator complexes. J. Biol. Chem. 274:1999;6667-6677.
32. Li D.S.et al. NRIF3 is a novel coactivator mediating functional specificity of nuclear hormone receptors. Mol. Cell. Biol. 19:1999;7191-7202.
33. Monden T.et al. Isolation and characterization of a novel ligand-dependent thyroid hormone receptor-coactivating protein. J. Biol. Chem. 272:1997;29834-29841.
34. Hörlein A.J.et al. Ligand-independent repression by the thyroid hormone receptor mediated by a nuclear receptor co-repressor. Nature. 377:1995;397-404.
35. Chen J.D., Evans R.M. A transcriptional co-repressor that interacts with nuclear hormone receptors. Nature. 377:1995;454-457.
36. Nagy L.et al. Nuclear receptor repression mediated by a complex containing SMRT, mSin3A, and histone deacetylase. Cell. 89:1997;373-380.
37. Ayer D.E.et al. Mad-Max transcriptional repression is mediated by ternary complex formation with mammalian homologs of yeast repressor Sin3. Cell. 80:1995;767-776.
38. Wagner B.L.et al. The nuclear corepressors NCoR and SMRT are key regulators of both ligand- and 8-bromo-cyclic AMP-dependent transcriptional activity of the human progesterone receptor. Mol. Cell. Biol. 18:1998;1369-1378.
39. Nan X.et al. Transcriptional repression by the methyl-CpG-binding protein MeCP2 involves a histone deacetylase complex. Nature. 393:1998;386-389.
40. Fondell J.D.et al. Unliganded thyroid hormone receptor alpha can target TATA-binding protein for transcriptional repression. Mol. Cell. Biol. 16:1996;281-287.
41. II70. Nucleic Acids Res. 26:1998;2899-2907.
42. Xu X., Lazar M.A. The CoRNR motif controls the recruitment of corepressors by nuclear hormone receptors. Nature. 402:1999;93-96.
43. Tagami T.et al. Nuclear receptor corepressors activate rather than suppress basal transcription of genes that are negatively regulated by thyroid hormone. Mol. Cell. Biol. 17:1997;2642-2648.
44. Tagami T.et al. Mechanisms that mediate negative regulation of the thyroid-stimulating hormone α gene by the thyroid hormone receptor. J. Biol. Chem. 274:1999;22345-22353.
45. Sasaki S.et al. Ligand-induced recruitment of a histone deacetylase in the negative-feedback regulation of the thyrotropin beta gene. EMBO J. 18:1999;5389-5398.