The Role of Histone Deacetylase 3 Complex in Nuclear Hormone Receptor Action

Overview

Journal Int J Mol Sci

Publisher MDPI

Specialties Biochemistry
Chemistry
Molecular Biology

Date 2021 Sep 10

PMID 34502048

Citations 10

Authors

Sumiyasu Ishii

Affiliations

Soon will be listed here.

Abstract

Nuclear hormone receptors (NRs) regulate transcription of the target genes in a ligand-dependent manner in either a positive or negative direction, depending on the case. Deacetylation of histone tails is associated with transcriptional repression. A nuclear receptor corepressor (N-CoR) and a silencing mediator for retinoid and thyroid hormone receptors (SMRT) are the main corepressors responsible for gene suppression mediated by NRs. Among numerous histone deacetylases (HDACs), HDAC3 is the core component of the N-CoR/SMRT complex, and plays a central role in NR-dependent repression. Here, the roles of HDAC3 in ligand-independent repression, gene repression by orphan NRs, NRs antagonist action, ligand-induced repression, and the activation of a transcriptional coactivator are reviewed. In addition, some perspectives regarding the non-canonical mechanisms of HDAC3 action are discussed.

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References

Bourguet W, Ruff M, Chambon P, Gronemeyer H, Moras D . Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-alpha. Nature. 1995; 375(6530):377-82. DOI: 10.1038/375377a0. View

Chen J, Evans R . A transcriptional co-repressor that interacts with nuclear hormone receptors. Nature. 1995; 377(6548):454-7. DOI: 10.1038/377454a0. View

Lawrence M, Daujat S, Schneider R . Lateral Thinking: How Histone Modifications Regulate Gene Expression. Trends Genet. 2015; 32(1):42-56. DOI: 10.1016/j.tig.2015.10.007. View

Li B, Carey M, Workman J . The role of chromatin during transcription. Cell. 2007; 128(4):707-19. DOI: 10.1016/j.cell.2007.01.015. View

Shibata H, Nawaz Z, Tsai S, OMalley B, Tsai M . Gene silencing by chicken ovalbumin upstream promoter-transcription factor I (COUP-TFI) is mediated by transcriptional corepressors, nuclear receptor-corepressor (N-CoR) and silencing mediator for retinoic acid receptor and thyroid hormone receptor.... Mol Endocrinol. 1997; 11(6):714-24. DOI: 10.1210/mend.11.6.0002. View

Mullican S, Gaddis C, Alenghat T, Nair M, Giacomin P, Everett L . Histone deacetylase 3 is an epigenomic brake in macrophage alternative activation. Genes Dev. 2011; 25(23):2480-8. PMC: 3243058. DOI: 10.1101/gad.175950.111. View

Lazar M, Hodin R, Darling D, Chin W . A novel member of the thyroid/steroid hormone receptor family is encoded by the opposite strand of the rat c-erbA alpha transcriptional unit. Mol Cell Biol. 1989; 9(3):1128-36. PMC: 362703. DOI: 10.1128/mcb.9.3.1128-1136.1989. View

Xu F, Zhang K, Grunstein M . Acetylation in histone H3 globular domain regulates gene expression in yeast. Cell. 2005; 121(3):375-85. DOI: 10.1016/j.cell.2005.03.011. View

Glass C, Rosenfeld M . The coregulator exchange in transcriptional functions of nuclear receptors. Genes Dev. 2000; 14(2):121-41. View

10.

. A unified nomenclature system for the nuclear receptor superfamily. Cell. 1999; 97(2):161-3. DOI: 10.1016/s0092-8674(00)80726-6. View

11.

Sun G, Yu R, Evans R, Shi Y . Orphan nuclear receptor TLX recruits histone deacetylases to repress transcription and regulate neural stem cell proliferation. Proc Natl Acad Sci U S A. 2007; 104(39):15282-7. PMC: 2000559. DOI: 10.1073/pnas.0704089104. View

12.

Perissi V, Aggarwal A, Glass C, Rose D, Rosenfeld M . A corepressor/coactivator exchange complex required for transcriptional activation by nuclear receptors and other regulated transcription factors. Cell. 2004; 116(4):511-26. DOI: 10.1016/s0092-8674(04)00133-3. View

13.

Huang P, Chandra V, Rastinejad F . Structural overview of the nuclear receptor superfamily: insights into physiology and therapeutics. Annu Rev Physiol. 2010; 72:247-72. PMC: 3677810. DOI: 10.1146/annurev-physiol-021909-135917. View

14.

Burcin M, Kohne A, Runge D, Steiner C, Renkawitz R . Factors influencing nuclear receptors in transcriptional repression. Semin Cancer Biol. 1994; 5(5):337-46. View

15.

Navabi N, Whitt J, Wu S, Woo V, Moncivaiz J, Jordan M . Epithelial Histone Deacetylase 3 Instructs Intestinal Immunity by Coordinating Local Lymphocyte Activation. Cell Rep. 2017; 19(6):1165-1175. PMC: 5499685. DOI: 10.1016/j.celrep.2017.04.046. View

16.

Urvalek A, Gudas L . Retinoic acid and histone deacetylases regulate epigenetic changes in embryonic stem cells. J Biol Chem. 2014; 289(28):19519-30. PMC: 4094062. DOI: 10.1074/jbc.M114.556555. View

17.

Somech R, Shaklai S, Geller O, Amariglio N, Simon A, Rechavi G . The nuclear-envelope protein and transcriptional repressor LAP2beta interacts with HDAC3 at the nuclear periphery, and induces histone H4 deacetylation. J Cell Sci. 2005; 118(Pt 17):4017-25. DOI: 10.1242/jcs.02521. View

18.

Villa R, Morey L, Raker V, Buschbeck M, Gutierrez A, De Santis F . The methyl-CpG binding protein MBD1 is required for PML-RARalpha function. Proc Natl Acad Sci U S A. 2006; 103(5):1400-5. PMC: 1360559. DOI: 10.1073/pnas.0509343103. View

19.

Grunstein M . Histone acetylation in chromatin structure and transcription. Nature. 1997; 389(6649):349-52. DOI: 10.1038/38664. View

20.

Seto E, Yoshida M . Erasers of histone acetylation: the histone deacetylase enzymes. Cold Spring Harb Perspect Biol. 2014; 6(4):a018713. PMC: 3970420. DOI: 10.1101/cshperspect.a018713. View