Coactivator and corepressor complexes in nuclear receptor function

Current Opinion in Genetics and Development

Volumn 9, Issue 2, 1999, Pages 140-147

  Lan, Xu ^a   Glass, Christopher K ^b   Rosenfeld, Michael G ^a  

^a HOWARD HUGHES MEDICAL INSTITUTE   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CELL NUCLEUS RECEPTOR; CYCLIC AMP RESPONSIVE ELEMENT BINDING PROTEIN; HISTONE ACETYLTRANSFERASE; HISTONE DEACETYLASE; HORMONE RECEPTOR; RETINOIC ACID RECEPTOR; THYROID HORMONE RECEPTOR; TRANSCRIPTION FACTOR;

CHROMATIN STRUCTURE; GENE ACTIVATION; GENE REPRESSION; HORMONE RECEPTOR INTERACTION; PRIORITY JOURNAL; REVIEW; TRANSCRIPTION REGULATION;

EID: 0033119162     PISSN: 0959437X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-437X(99)80021-5     Document Type: Article

References (57)

1. Horlein AJ, Näär AM, Heinzel T, Torchia J, Gloss B, Kurokawa R, Ryan A, Kamei Y, Seoderstreom M, Glass CK, Rosenfeld MG: Ligand-independent repression by the thyroid hormone receptor mediated by a nuclear receptor co-repressor. Nature 1995, 377:397-404.
2. Chen JD, Evans RM: A transcriptional co-repressor that interacts with nuclear hormone receptors. Nature 1995, 377:454-457.
3. HOng H, KOhli K, Garabedian MJ, Stallcup MR: GRIP1, a transcriptional coactivator for the AF-2 transactivation domain of steroid, thyroid, retinoid, and vitamin D receptors. Mol Cell Biol 1997, 17:2735-2744.
4. Voegel JJ, Heine MJS, Tini M, Vivat V, Chambon P, Gronemeyer H: The coactivator TIF2 contains three nuclear receptor-binding motifs and mediates transactivation through CBP binding-dependent and -independent pathways. EMBO J 1998, 17:507-519.
5. Torchia J, Rose DW, Inostroza J, Kamei Y, Westin S, Glass CK, Rosenfeld MG: The transcriptional co-activator p/CIP binds CBP and mediates nuclear-receptor function. Nature 1997, 387:677-684.
6. Chen HW, Lin RJ, Schiltz RL, Chakravarti D, Nash A, Nagy L, Privalsky ML, Nakatani Y, Evans RM: Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300. Cell 1997, 90:569-580.
7. Anzick SL, Kononen J, Walker RL, Azorsa DO, Tanner MM, Guan XY, Sauter G, Kallioniemi OP, Trent JM, Meltzer PS: AIB1, a steroid receptor coactivator amplified in breast and ovarian cancer. Science 1997, 277:965-968.
8. Kamei Y, Xu L, Heinzel T, Torchia J, Kurokawa R, Gloss B, Lin SC, Heyman RA, Rose DW, Glass CK, Rosenfeld MG: A CBP integrator complex mediates transcriptional activation and AP-1 inhibition by nuclear receptors. Cell 1996, 85:403-414.
9. Chakravarti D, Lamorte VJ, Nelson MC, Nakajima T, Schulman IG, Juguilon H, Montminy M, Evans RM: Role of CBP/p300 in nuclear receptor signalling. Nature 1996, 383:99-103.
10. Blanco JCG, Minucci S, Lu JM, Yang XJ, Walker KK, Chen HW, Evans RM, Nakatani Y, Ozato K: The histone acetylase PCAF is a nuclear receptor coactivator. Genes Dev 1998, 12:1638-1651. This paper describes direct intereaction between p/CAF and nuclear receptors which is independent of the ligand-induced association between nuclear receptors and NCoAs or CBP/p300. The authors also provides evidence supporting the role of p/CAF in nuclear receptor mediated activation of gene expression.
11. Korzus E, Torchia J, Rose DW, Xu L, Kurokawa R, McInerney Em, Mullen TM, Glass CK, Rosenfeld MG: Transcription factor-specific requirements for coactivators and their acetyltransferase functions. Science 1998, 279:703-707. In this study, the requirement for p/CAF in transactivation events mediated by several families of transcription factors are assessed. The data reveals separate interactions between p/CAF with CBP and NCoAs. Functional evidence suggests a differential requirement for p/CAF and HAT functions by different families of transcription factors.
12. Struhl K: Histone acetylation and transcriptional regulatory mechanisms. Genes Dev 1998, 12:599-606.
13. Kadonaga JT: Eukaryotic transcription: An interlaced network of transcription factors and chromatin-modifying machines. Cell 1998,92:307-313. An insightful review on the relationship between chromatin modification and its impact on gene regulation.
14. Bannister AJ, Kouzarides T: The CBP co-activator is a histone acetyltransferase. Nature 1996, 384:641-643.
15. Ogryzko VV, Schiltz RL, Russanova V, Howard BH, Nakatani Y: The transcriptional coactivators p300 and CBP are histone acetyltransferases. Cell 1996, 87:953-959.
16. Yang XJ, Ogryzko VV, Nishikawa J, Howard BH, Nakatani Y: A p300/CBP- associated factor that competes with the adenoviral oncoprotein E1a. Nature 1996, 382:319-324.
17. Spencer TE, Jenster G, Burcin MM, Allis CD, Zhou JX, Mizzen CA, McKenna NJ, Onate SA, Tsai SY, Tsai MJ, O'Malley BW: Steroid receptor coactivator-1 is a histone acetyltransferase. Nature 1997, 389:194-198. The first report on in vitro evidence indicating the intrinsic HAT activity of SRC-1/NCoA-1.
18. Heinzel T, Lavinsky RM, Mullen TM, Soderstrom M, Laherty CD, Torchia J, Yang WM, Brard G, Ngo SD, Davie JR et al.: A complex containing N-CoR, mSin3 and histone deacetylase mediates transcriptional repression. Nature 1997, 387:43-48. This study demonstrates an interaction between NCoR/SMRT with the genetically defined Sin3 corepressor. Furthermore, HDAC activities are also found to be crucial components of this complex which is required for repression by unliganded nuclear receptors and Mad.
19. Nagy L, Kao HY, Chakravarti D, Lin RJ, Hassig CA, Ayer DE, Schreiber SL, Evans RM: Nuclear receptor repression mediated by a complex containing SMRT, mSin3A, and histone deacetylase. Cell 1997, 89:373-380. A similar report to [18•], which suggests that the HDAC-containing SMRT/mSin3 complex plays a crucial role in repression by unliganded nuclear receptors.
20. Lavinsky RM, Jepsen K, Heinzel T, Torchia J, Mullen TM, Schiff R, DelRio AL, Ricote M, Ngo S, Gemsch J et al.: Diverse signaling pathways modulate nuclear receptor recruitment of N-CoR and SMRT complexes. Proc Natl Acad Sci USA 1998, 95:2920-2925. This study shows an interaction between NCoR and antagonist-bound ER. Moreover, the authors provide evidence indicating that activation of the cAMP-signaling pathway resulted in loss of ER-NCoR interaction, and functionally converts antagonist such as tamoxifen into an agonist.
21. Woloshin P, Song K, Degnin C, Killary AM, Goldhamer DJ, Sassoon D, Thayer MY: Msx-1 inhibits Myo-D expression in fibroblast x 1OT1/2 cell hybrids. Cell 1995, 82:611-620.
22. Kao HY, Ordentlich P, Koyano-Nakagawa N, Tang Z, Downes M, Kintner CR, Evans RM, Kadesch T: A histone deacetylase corepressor complex regulates the Notch signal transduction pathway. Genes Dev 1998, 12:2269-2277.
23. Zhang Y, Sun ZW, Iratni R, Erdjument-Bromage H, Tempst P, Hampsey M, Reinberg D: SAP30, a novel protein conserved between human and yeast, is a component of a histone deacetylase complex. Mol Cell 1998, 1:1021-1031. The purification of a core mSin3 complex, and identification of the p30 component of this complex. Characterization of other components of this complex is also described.
24. Laherty CD, Billin AN, Lavinsky RM, Yochum GS, Bush AC, Sun JM, Mullen TM, Davie JR, Rose DW, Glass CK et al.: SAP30, a component of the mSin3 corepressor complex involved in N-CoR-mediated repression by specific transcription factors. Mol Cell 1998, 2:33-42. This study describes the isolation and functional characterization of the p30 component of the mSin3 complex.
25. Zhang Y, LeRoy G, Seelig H-P, Lane WS, Reinberg D: The dermatomyositis-Specific autoantigen Mi2 is a component of a complex containing histone deacetylase and nucleosome remodeling activities. Cell 1998, 95:279-289. The purification of a core HDAC complex, and identification of Mi2 as a component of this complex. Characterization of some of the other components of this complex are also described.
26. Tong JK, Hassig CA, Schnitzler GR, Kingston RE, Schreiber SL: Chromatin deacetylation by an ATP-dependent nucleosome remodelling complex. Nature 1998, 395:917-921. This paper describes the isolation and functional characterization of a HDAC complex (termed NRD) containing ATP-dependent nucleosome-remodelling activity. The CH D3 and CHD4 proteins of this complex harbor helicase/ATPase domains and facilitate the deacetylation of oligonucleosomal histones in vitro.
27. Zhang J, Guenther MG, Carthew RW, Lazar MA: Proteasomal regulation of nuclear receptor corepressor-mediated repression. Genes Dev 1998, 12:1775-1780. This study suggests a proteolytic regulation of NCoR by mSiah2, which presents a novel way of controling transcriptional repression.
28. Chrivia JC, Kwok RPS, Lamb N, Hagiwara M, Montminy MR, Goodman RH: Phosphorylated CREB binds specifically to the nuclear protein CBP. Nature 1993, 365:855-859.
29. Eckner R, Ewen ME, Newsome D, Gerdes M, DeCaprio JA, Lawrence JB, Livingston DM: Molecular cloning and functional analysis of the adenovirus E1A- associated 300-kd protein (p300) reveals a protein with properties of a transcriptional adaptor. Genes Dev 1994, 8:869-884.
30. Shikama N, Lyon J, LaThangue NB: The p300/CBP family: Integrating signals. With transcription factors and chromatin. Trends Cell Biol 1997, 7:230-236. One of the most complete summaries of reseach on CBP/p300.
31. -/- mice. The data supported, among other functions such as growth regulation, the belief that p300 is a key component of RA-mediated gene activation event. Study of heterozygous animals also revealed that the level of cellular p300 is rate-limiting and crucial for embryonic development. This finding supports the previous hypothesis that partitioning of rate-limiting CBP/p300 would result in transrepression among different transcription factors.
32. Kawasaki H, Eckner R, Yao TP, Taira K, Chiu R, Livingston DM, Yokoyama KK: Distinct roles of the co-activators p300 and CBP in retinoic-acid-induced F9-cell differentiation. Nature 1998, 393:284-289. An elegant study utilizing hammerhead ribozyme targeting specifically either CBP or p300. The data not only confirms the idea that CBP and p300 are required for RA-induced gene expression but also reveals that CBP and p300 are differentially required for different RA-inducible genes in the cell. This is the first evidence suggesting differences in physiological functions between biochemically similar CBP and p300.
33. Naar AM, Beaurang PA, Robinson KM, Oliner JD, Avizonis D, Scheek S, Zwicker J, Kadonaga JT, Tjian R: Chromatin, TAFs, and a novel multiprotein coactivator are required for synergistic activation by Sp1 and SREBP-1a in vitro. Genes Dev 1998,12:3020-3031. The first description of a high-affinity CBP-containing complex that is able to support synergy between Sp1 and SREBP-1a only on a chromatin template in vitro. Identities of subunits of this complex remain unknown.
34. Kraus WL, Kadonaga JT: P300 and estrogen receptor cooperatively activate transcription via differential enhancement of initiation and reinitiation. Genes Dev 1998, 12:331-342. The authors here establish the first in vitro system mimicking ligand-induced transcriptional activation by estrogen receptor. Using this assay, the authors demonstrate that purified p300 potentiated estrogen receptor mediates transcription from a chromatinized template in a ligand-dependent manner.
35. Nakajima T, Uchida C, Anderson SF, Lee CG, Hurwitz J, Parvin JD, Montminy M: RNA helicase A mediates association of CBP with RNA polymerase II. Cell 1997, 90:1107-1112.
36. Xu L, Lavinsky RM, Dasen JS, Flynn SE, McInerney EM, Mullen TM, Heinzel T, Szeto D, Korzus E, Kurokawa R et al: Signal-specific co-activator domain requirements for Pit-1 activation. Nature 1998, 395:301-306. This study suggests that the displacement of NCoR by CBP also underlies the activity of Pit-1, a POU homeodomain transcription factor. Moreover, the authors also provide evidence indicating that Pit-1 function is stimulated by different signaling pathways and for each pathway the required CBP domains are different. These observations suggest that the assembly of CBP complexes are modified by signal-induced phosphorylation events (see also [37••]).
37. Chawla S, Hardingham GE, Quinn DR, Bading H: CBP: A signal-regulated transcriptional coactivator controlled by nuclear calcium and CaM kinase IV. Science 1998, 281:1505-1509. Another study which, as with [36••], indicates that CBP, and/or its associated partners, are regulated by signal transduction pathways.
38. Yao TP, Ku G, Zhou N, Scully R, Livingston DM: The nuclear hormone receptor coactivator SRC-1 is a specific target of p300. Proc Natl Acad Sci USA 1996, 93:10626-10631.
39. Heery DM, Kalkhoven E, Hoare S, Parker MG: A signature motif in transcriptional co-activators mediates binding to nuclear receptors. Nature 1997, 387:733-736.
40. McInerney EM, Rose DW, Flynn SE, Westin S, Mullen T-M, Krones A, Inostroza J, Torcia J, Assa-MuNt N, Milburn MV et al.: Determinants of coactivator LXXLL motif specificity in nuclear receptor transcriptional activation. Genes Dev 1998, 12:3357-3368. Extensive mutagenesis analysis of the LXXLL motifs in SRC-1/NCoA-1. Functional evidence suggests that different LXXLL motifs are involved in supporting different nuclear receptors in transcription. The specificities appear to reside in the residues located carboxy-terminal to the LXXLL motif.
41. -/- mice are generated in this study; these mice exhibit some abnormalities in a few organs such as uterus, prostate, testis and mammary gland. In addition, the authors observed an upregulation of TIF2/GRIP1 /NCoA-2 in these animals, suggesting compensation of loss of SRC-1 by NCoA family members.
42. Nolle RT, Wisely GB, Westin S, Cobb JE, Lambert MH, Kurokawa R, Rosenfeld MG, Willson TM, Glass CK, Milburn MV: Ligand binding and co-activator assembly of the peroxisome proliferator-activated receptor-γ. Nature 1998, 395:137-143. An important study of a co-crystal of ligand-bound PPARγ homodimer and a fragment of SRC-1/NCoA-1 including two LXXLL motifs. Structural analysis provided substantial information regarding the structure of the ligand-binding pocket, the LXXLL interaction interface, and conformation of the homodimer.
43. Darimont BD, Wagner RL, Apriletti JW, Stallcup MR, Kushner PJ, Baxter JD, Fletterick RJ, Yamamoto KR: Structure and specificity of nuclear receptor-coactivator interactions. Genes Dev 1998, 12:3343-3356. Biochemical and crystallographic analysis of the ligand-binding domain of TR and an LXXLL motif from GRIP1. Structural elements determining the specific interaction between TR and the LXXLL motif of GRIP1 are revealed.
44. Westin S, Kurokawa R, Nolte RT, Wisely GB, McInerney EM, Rose DW, Milburn MV, Rosenfeld MG, Glass CK: Interactions controlling the assembly of nuclear- receptor heterodimers and co-activators. Nature 1998, 395:199-202. Based on the structural modeling of RAR-RXR heterodimer with SRC-1/NCoA-1, the authors here provide biochemical evidence suggesting that SRC-1/NCoA-1 recruitment by liganded RAR allows RXR to bind to its ligand, which subsequently would interact with a second LXXLL motif of the same SRC-1/NCoA-1 molecule. This explains synergy between RAR and RXR ligands in vivo.
45. Puri PL, Sartorelli V, Yang XJ, Hamamori Y, Ogryzko VV, Howard BH, Kedes L, Wang JYJ, Graessmann A, Nakatani Y, Levrero M: Differential roles of p300 and PCAF acetyltransferases in muscle differentiation. Mol Cell 1997, 1:35-45.
46. Ogryzko VV, Kotani T, Zhang XL, Schiltz RL, Howard T, Yang XJ, Howard BH, Qin J, Nakatani Y: Histone-like TAFs within the pCAF histone acetylase complex. Cell 1998, 94:35-44. This paper describes the purification of a core p/CAF complex, revealing TAFs, TAF-like molecules and histone like molecules as constituents. These associated partners potentiate the histone acetylation acitivity of p/CAF on nucleosomal substrates.
47. Grant PA, Duggan L, Caotae J, Roberts SM, Brownell JE, Candau R, Ohba R, Owen-Hughes T, Allis CD, Winston F et al.: Yeast Gcn5 functions in two multisubunit complexes to acetylate nucleosomal histones: Characterization of an Ada complex and the SAGA Spt/Ada complex. Genes Dev 1997, 11:1640-1650.
48. Fondell JD, Ge H, Roeder RG: Ligand induction of a transcriptionally active thyroid hormone receptor coactivator complex. Proc Natl Acad Sci USA 1996, 93:8329-8333.
49. Rachez C, Suldan Z, Ward J, Chang CPB, Burakov D, Erdjument-Bromage H, Tempst P, Freedman LP: A novel protein complex that interacts with the vitamin D-3 receptor in a ligand-dependent manner and enhances VDR transactivation in a cell-free system. Genes Dev 1998, 12:1787-1800. This study describes the purification of a HAT-containing complex bound to a number of nuclear receptors in response to ligands. This complex supports nuclear receptor mediated transcription from the naked DNA template and does not include CBP/p300, NCoAs or p/CAF.
50. Rachez C, Lemon BD, Suldan Z, Bromleigh V, Gamble M, Näär AM, Bromage HE, Tempst P, Freedman LP: Nuclear receptors require the DRIP complex for ligand-dependent transactivation on chromatin templates. Nature 1999, in press. Molecular characterization of the DRIP complex, revealing its resemblance to the ARC complex (see [51••]). Functionally demonstrated that the highly purified DRIP complex is required for ligand-dependent transcriptional activation by VDR on chromatin template in vitro.
51. Näär AM, Beaurang PA, Zhou S, Abrahams S, Solomon W, Tijan R: Composite coactivator ARC mediates chromatin-directed transcriptional activation. Nature 1999, in press. Molecular characterization and functional examination of the ARC. ARC appeared to be capable of supporting multiple families of transcriptional factor on chromatin template.
52. Li Y, Bjorklund S, Jiang YW, Kim YJ, Lane WS, Stillman DJ, Komberg RD: Yeast global transcriptional regulators Sin4 and Rgr1 are components of mediator complex/RNA polymerase II holoenzyme. Proc Natl Acad Sci USA 1995, 92:10864-10868.
53. Wong J, Shi YB, Wolffe AP: Determinants of chromatin disruption and transcriptional regulation instigated by the thyroid hormone receptor: Hormone-regulated chromatin disruption is not sufficient for transcriptional activation. EMBO J 1997, 16:3158-3171.
54. Ostlund Farrants AK, Blomquist P, Kwon H, Wrange O: Glucocorticoid receptor- glucocorticoid response element binding stimulates nucleosome disruption by the SWI/SNF complex. Mol Cell Biol 1997, 17:895-905.
55. Puigserver P, Wu Z, Park CW, Graves R, Wright M, Spiegelman BM: A cold- inducible coactivator of nuclear receptors linked to adaptive thermogenesis. Cell 1998, 92:829-839. The report of the first tissue-specific, and inducible coactivator for a nuclear receptor. It is unclear if it has target gene specificity.
56. Hansen SK, Takada S, Jacobson RH, Lis JT, Tjian R: Transcription properties of a cell type-specific TATA-binding protein, TRF. Cell 1997,91:71-83. This paper reports functional analysis of a second TATA-binding protein and the factors associated with it. TRF is functionally similar to TBP, but is restricted to specific cell types and is localized to distinct loci in vivo. The presented evidence suggests that the TRF complex is targeted to activate specific genes.
57. Sif S, Stukenberg PT, Kirschner MW, Kingston RE: Mitotic inactivation of a human SWI/SNF chromatin remodeling complex. Genes Dev 1998, 12:2842-2851. The authors here report cell-cycle-dependent regulation of the SWI/SNF complex. Phosphorylation of some components of this complex leads to inactivation of its chromatin-remodeling function.