Modulation of nuclear receptor dependent transcription

Biological Research

Volumn 35, Issue 2, 2002, Pages 295-303

  Hart, Stephen M ^a  

^a IMPERIAL COLLEGE LONDON   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ANDROGEN RECEPTOR; CELL NUCLEUS RECEPTOR; DIMER; DNA; ESTROGEN RECEPTOR ALPHA; LIGAND; RETINOIC ACID RECEPTOR ALPHA; TRANSCRIPTION FACTOR;

ANIMAL CELL; ARTICLE; BREAST CANCER; CHROMATIN STRUCTURE; COMPLEX FORMATION; CONTROLLED STUDY; DNA RESPONSIVE ELEMENT; GENE ACTIVATION; GENE EXPRESSION REGULATION; GENE REPRESSION; GENE TARGETING; GENETIC TRANSCRIPTION; HUMAN; HUMAN CELL; LEUKEMIA; NONHUMAN; PATHOGENESIS; PROSTATE CANCER; PROTEIN DNA BINDING; PROTEIN FAMILY; PROTEIN FUNCTION;

ANIMALIA; EUKARYOTA; HOMO;

EID: 0036400759     PISSN: 07169760     EISSN: None     Source Type: Journal    
DOI: 10.4067/S0716-97602002000200021     Document Type: Article

References (59)

1. ALEN P, CLAESSENS F, SCHOENMAKERS E, SWINNEN JV, VERHOEVEN G, ROMBAUTS W, PEETERS B (1999) Interaction of the putative androgen receptor-specific coactivator ARA70/ELE1alpha with multiple steroid receptors and identification of an internally deleted ELE1beta isoform. Mol Endocrinol 13: 117-128
2. ALLAND L, MUHLE R, HOU H, JR., POTES J, CHIN L, SCHREIBER-AGUS N, DEPINHO RA (1997) Role for N-CoR and histone deacetylase in Sin3-mediated transcriptional repression. Nature 387:49-55
3. BANIAHMAD A, KOHNE AC, RENKAWITZ R (1992) A transferable silencing domain is present in the thyroid hormone receptor, in the v-erbA oncogene product and in the retinoic acid receptor. EMBO J 11:1015-1023
4. BANIAHMAD A, LENG X, BURRIS TP, TSAI SY, TSAI MJ, OMALLEY BW, 1995. The tau 4 activation domain of the thyroid hormone receptor is required for release of a putative corepressor(s) necessary for transcriptional silencing. Mol Cell Biol 15:76-86
5. BLANCO JC, MINUCCI S, LU J, YANG XJ, WALKER KK, CHEN H, EVANS RM, NAKATANI Y, OZATO K (1998) The histone acetylase PCAF is a nuclear receptor coactivator. Genes Dev 12: 1638-1651
6. BURAKOV D, WONG CW, RACHEZ C, CHESKIS BJ, FREEDMAN LP (2000) Functional interactions between the estrogen receptor and DRIP205, a subunit of the heteromeric DRIP coactivator complex. J Biol Chem 275:20928-20934
7. CASANOVA J, HELMER E, SELMI-RUBY S, QI IS, AUFLIEGNER M, DESAI-YAJNIK V, KOUDINOVA N, YARM F, RAAKA BM, SAMUELS HH (1994) Functional evidence for ligand-dependent dissociation of thyroid hormone and retinoic acid receptors from an inhibitory cellular factor. Mol Cell Biol 14:5756-5765
8. CHEN JD, EVANS RM (1995) A transcriptional corepressor that interacts with nuclear hormone receptors. Nature 377:454-457
9. COUETTE B, FAGART J, JALAGUIER S, LOMBES M, SOUQUE A, RAFESTIN-OBLIN ME (1996) Ligand-induced conformational change in the human mineralocorticoid receptor occurs within its hetero-oligomeric structure. Biochem J 315 (Pt 2):421-427
10. DIRENZO J, SHANG Y, PHELAN M, SIF S, MYERS M, KINGSTON R, BROWN M (2000) BRG-1 is recruited to estrogen-responsive promoters and cooperates with factors involved in histone acetylation. Mol Cell Biol 20:7541-7549
11. DRISCOLL JE, SEACHORD CL, LUPISELLA JA, DARVEAU RP, RECZEK PR (1996) Ligand-induced conformational changes in the human retinoic acid receptor detected using monoclonal antibodies. J Biol Chem 271:22969-22975
12. FONDELL JD, GE H, ROEDER RG (1996) Ligand induction of a transcriptionally active thyroid hormone receptor coactivator complex. Proc Natl Acad Sci USA 93:8329-8333
13. FRYER CJ, ARCHER TK (1998) Chromatin remodelling by the glucocorticoid receptor requires the BRG1 complex. Nature 393:88-91
14. GIGUERE V (1999) Orphan nuclear receptors: from gene to function. Endocr Rev 20:689-725
15. GLASS CK, ROSENFELD MG (2000) The coregulator exchange in transcriptional functions of nuclear receptors. Genes Dev 14:121-141
16. GROZINGER CM, HASSIG CA, SCHREIBER SL (1999) Three proteins define a class of human histone deacetylases related to yeast Hdalp. Proc Natl Acad Sci USA 96:4868-4873
17. GUENTHER MG, BARAK O, LAZAR MA (2001) The SMRT and N-CoR corepressors are activating cofactors for histone deacetylase 3. Mol Cell Biol 21:6091-6101
18. GUENTHER MG, LANE WS, FISCHLE W, VERDIN E, LAZAR MA, SHIEKHATTAR R (2000) A core SMRT corepressor complex containing HDAC3 and TBL1, a WD40-repeat protein linked to deafness. Genes Dev 14:1048-1057
19. HASSIG CA, FLEISCHER TC, BILLIN AN, SCHREIBER SL, AYER DE (1997) Histone deacetylase activity is required for full transcriptional repression by mSin3A. Cell 89:341-347
20. HEERY DM, KALKHOVEN E, HOARE S, PARKER MG (1997) A signature motif in transcriptional coactivators mediates binding to nuclear receptors. Nature 387:733-736
21. HEINZEL T, LAVINSKY RM, MULLEN TM, SODERSTROM M, LAHERTY CD, TORCHIA J, YANG WM, BRARD G, NGO SD, DAVIE JR, SETO E, EISENMAN RN, ROSE DW, GLASS CK, ROSENFELD MG (1997) A complex containing N-CoR, mSin3 and histone deacetylase mediates transcriptional repression. Nature 387:43-48
22. HORLEIN AJ, NAAR AM, HEINZEL T, TORCHIA J, GLOSS B, KUROKAWA R, RYAN A, KAMEI Y, SODERSTROM M, GLASS CK (1995) Ligand-independent repression by the thyroid hormone receptor mediated by a nuclear receptor co-repressor. Nature 377:397-404
23. HU X, LAZAR MA (1999) The CoRNR motif controls the recruitment of corepressors by nuclear hormone receptors. Nature 402:93-96
24. HU X, LI Y, LAZAR MA (2001) Determinants of CoRNR-dependent repression complex assembly on nuclear hormone receptors. Mol Cell Biol 21:1747-1758
25. HUANG EY, ZHANG J, MISKA EA, GUENTHER MG, KOUZARIDES T, LAZAR MA (2000) Nuclear receptor corepressors partner with class II histone deacetylases in a Sin3-independent repression pathway. Genes Dev 14:45-54
26. JACKSON TA, RICHER JK, BAIN DL, TAKIMOTO GS, TUNG L, HORWITZ KB (1997) The partial agonist activity of antagonist-occupied steroid receptors is controlled by a novel hinge domain-binding coactivator L7/SPA and the corepressors N-CoR or SMRT. Mol Endocrinol 11:693-705
27. JENSTER G, SPENCER TE, BURCIN MM, TSAI SY, TSAI MJ, OMALLEY BW (1997) Steroid receptor induction of gene transcription: a two-step model. Proc Natl Acad Sci USA 94:7879-7884
28. JENSTER G, VAN DER KORPUT HA, TRAPMAN J, BRINKMANN AO (1995) Identification of two transcription activation units in the N-terminal domain of the human androgen receptor. J Biol Chem 270:7341-7346
29. KAO HY, DOWNES M, ORDENTLICH P, EVANS RM (2000) Isolation of a novel histone deacetylase reveals that class I and class II deacetylases promote SMRT-mediated repression. Genes Dev 14:55-66
30. KLINGE CM (2000) Estrogen receptor interaction with co-activators and co-repressors. Steroids 65:227-251
31. KNOEPFLER PS, EISENMAN RN (1999) Sin meets NuRD and other tails of repression. Cell 99:447-450
32. LAHERTY CD, BILLIN AN, LAVINSKY RM, YOCHUM GS, BUSH AC, SUN JM, MULLEN TM, DAVIE JR, ROSE DW, GLASS CK, ROSENFELD MG, AYER DE, EISENMAN RN (1998) SAP30, a component of the mSin3 corepressor complex involved in N-CoR-mediated repression by specific transcription factors. Mol Cell 2:33-42
33. LANZ RB, MCKENNA NJ, ONATE SA, ALBRECHT U, WONG J, TSAI SY, TSAI MJ, O'MALLEY BW (1999) A steroid receptor coactivator, SRA, functions as an RNA and is present in an SRC-1 complex. Cell 97:17-27
34. LOVE JD, GOOCH JT, NAGY L, CHATTERJEE VK, SCHWABE JW (2000) Transcriptional repression by nuclear receptors: mechanisms and role in disease. Biochem Soc Trans 28:390-396
35. MANGELSDORF DJ, THUMMEL C, BEATO M, HERRLICH P, SCHUTZ G, UMESONO K, BLUMBERG B, KASTNER P, MARK M, CHAMBON P (1995) The nuclear receptor superfamily: the second decade. Cell 83:835-839
36. MCKENNA NJ, O'MALLEY BW (2000) An issue of tissues: divining the split personalities of selective estrogen receptor modulators. Nat Med 6:960-962
37. MORAS D, GRONEMEYER H (1998) The nuclear receptor ligand-binding domain: structure and function. Curr Opin Cell Biol 10:384-391
38. NAAR AM, BEAURANG PA, ZHOU S, ABRAHAM S, SOLOMON W, TJIAN R (1999) Composite co-activator ARC mediates chromatin-directed transcriptional activation. Nature 398:828-832
39. NAGY L, KAO HY, CHAKRAVARTI D, LIN RJ, HASSIG CA, AYER DE, SCHREIBER SL, EVANS RM (1997) Nuclear receptor repression mediated by a complex containing SMRT, mSin3A, and histone deacetylase. Cell 89:373-380
40. NAGY L, KAO HY, LOVE JD, LI C, BANAYO E, GOOCH JT, KRISHNA V, CHATTERJEE K, EVANS RM, SCHWABE JW (1999) Mechanism of corepressor binding and release from nuclear hormone receptors. Genes Dev 13:3209-3216
41. NICHOLS M, RIENTJES JM, STEWART AF (1998) Different positioning of the ligand-binding domain helix 12 and the F domain of the estrogen receptor accounts for functional differences between agonists and antagonists. EMBO J 17:765-773
42. NOMURA T, KHAN MM, KAUL SC, DONG HD, WADHWA R, COLMENARES C, KOHNO I, ISHII S (1999) Ski is a component of the historic deacetylase complex required for transcriptional repression by Mad and thyroid hormone receptor. Genes Dev 13:412-423
43. OLEFSKY JM (2001) Nuclear receptor minireview series. J Biol Chem 276:36863-36864
44. PARKER MG (1993) Steroid and related receptors. Curr Opin Cell Biol 5:499-504
45. PARTHUN MR, WIDOM J, GOTTSCHLING DE (1996) The major cytoplasmic histone acetyltransferase in yeast: links to chromatin replication and histone metabolism. Cell 87:85-94
46. PERLMANN T, RANGARAJAN PN, UMESONO K, EVANS RM (1993) Determinants for selective RAR and TR recognition of direct repeat HREs. Genes Dev 7:1411-1422
47. RACHEZ C, SULDAN Z, WARD J, CHANG CP, BURAKOV D, ERDJUMENT-BROMAGE H, TEMPST P, FREEDMAN LP (1998) A novel protein complex that interacts with the vitamin D3 receptor in a ligand-dependent manner and enhances VDR transactivation in a cell-free system. Genes Dev 12:1787-1800
48. SHIAU AK, BARSTAD D, LORIA PM, CHENG L, KUSHNER PJ, AGARD DA, GREENE GL (1998) The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interaction by tamoxifen. Cell 95:927-937
49. SMITH CL, NAWAZ Z, O'MALLEY BW (1997) Coactivator and corepressor regulation of the agonist/antagonist activity of the mixed antiestrogen, 4-hydroxytamoxifen. Mol Endocrinol 11: 657-666
50. TAGAMI T, JAMESON JL (1998) Nuclear corepressors enhance the dominant negative activity of mutant receptors that cause resistance to thyroid hormone. Endocrinology 139:640-650
51. TANENBAUM DM, WANG Y, WILLIAMS SP, SIGLER PB (1998) Crystallographic comparison of the estrogen and progesterone receptor's ligand binding domains. Proc Natl Acad Sci USA 95:5998-6003
52. TAUNTON J, HASSIG CA, SCHREIBER SL (1996) A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p. Science 272:408-411
53. TREUTER E, JOHANSSON L, THOMSEN JS, WARNMARK A, LEERS J, PELTO-HUIKKO M, SJOBERG M, WRIGHT AP, SPYROU G, GUSTAFSSON JA (1999) 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 274:6667-6677
54. WEBB P, NGUYEN P, SHINSAKO J, ANDERSON C, FENG W, NGUYEN MP, CHEN D, HUANG SM, SUBRAMANIAN S, MCKINERNEY E, KATZENELLENBOGEN BS, STALLCUP MR, KUSHNER PJ (1998) Estrogen receptor activation function 1 works by binding p160 coactivator proteins. Mol Endocrinol 12:1605-1618
55. WILKINSON JR, TOWLE HC (1997) Identification and characterization of the AF-1 transactivation domain of thyroid hormone receptor beta1. J Biol Chem 272:23824-23832
56. YUAN CX, ITO M, FONDELL JD, FU ZY, ROEDER RG (1998) The TRAP220 component ofa thyroid hormone receptor-associated protein (TRAP) coactivator complex interacts directly with nuclear receptors in a ligand-dependent fashion. Proc Natl Acad Sci USA 95:7939-7944
57. ZECHEL C, SHEN XQ, CHAMBON P, GRONEMEYER H (1994) Dimerization interfaces formed between the DNA binding domains determine the cooperative binding of RXR/RAR and RXR/TR heterodimers to DR5 and DR4 elements. EMBO J 13:1414-1424
58. ZHANG Y, IRATNI R, ERDJUMENT-BROMAGE H, TEMPST P, REINBERG D (1997) Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex. Cell 89:357-364
59. ZHU Y, QI C, JAIN S, RAO MS, REDDY JK (1997) Isolation and characterization of PBP, a protein that interacts with peroxisome proliferator-activated receptor. J Biol Chem 272:25500-25506