The histone deacetylase-3 complex contains nuclear receptor corepressors

Wen, Yu‐Der; Perissi, Valentina; Staszewski, Lena M.; Yang, Wen‐Ming; Krones, Anna; Glass, Christopher K.; Rosenfeld, Michael G.; Seto, Edward

doi:10.1073/pnas.97.13.7202

Cited by 323 publications

(274 citation statements)

References 32 publications

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“…A similar combination of class II and class III enzymes in a multiprotein complex was recently observed for HDAC6 and SIRT2, a human class III HDAC [56]. SMRTand N-CoR interact both with class IIa HDACs and with HDAC3 through distinct domains [52,53,57,58], an observation that explains why class IIa HDACs coimmunoprecipitate with HDAC3 [5,16,48]. Class IIa HDACs are enzymatically inactive alone as purified recombinant proteins.…”

Section: Dynamic Subcellular Localizationsupporting

confidence: 61%

Class II histone deacetylases: versatile regulators

2003

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Histone acetylation and deacetylation play essential roles in modifying chromatin structure and regulating gene expression in eukaryotes. Histone deacetylases (HDACs) catalyze the deacetylation of lysine residues in the histone N-terminal tails and are found in large multiprotein complexes with transcriptional co-repressors. Human HDACs are grouped into three classes based on their similarity to known yeast factors: class I HDACs are similar to the yeast transcriptional repressor yRPD3, class II HDACs to yHDA1 and class III HDACs to ySIR2. In this review, we focus on the biology of class II HDACs. These newly discovered enzymes have been implicated as global regulators of gene expression during cell differentiation and development. We discuss their emerging biological functions and the molecular mechanisms by which they are regulated.

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Section: Dynamic Subcellular Localizationsupporting

confidence: 61%

Class II histone deacetylases: versatile regulators

2003

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“…SUMOylation of Elk-1, for example, results in the recruitment of histone deacetylase activity, in particular HDAC-2, to promoters (Yang and Sharrocks, 2004). The N-terminal portion of NCoR interacts with HDAC3 and Sin3A (Heinzel et al, 1997;Guenther et al, 2000;Wen et al, 2000). We could not observe any SUMOylation-induced changes in the binding of these proteins to N-CoR ( Figure 6C and unpublished data).…”

Section: Discussionmentioning

confidence: 69%

SUMOylation of the Corepressor N-CoR Modulates Its Capacity to Repress Transcription

Tiefenbach

Novac

Ducasse

et al. 2006

MBoC

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“…Biochemical purifications of both N-CoR/SMRT as well as HDAC3-associated proteins, mostly based on immunoaffinity precipitation followed by mass spectrometry, converged to this conclusion Wen et al, 2000;Li et al, 2000;Zhang et al, 2002;Yoon et al, 2003). At least in HeLa cells, the majority of cellular HDAC3 is found to associate with SMRT and N-CoR complexes.…”

Section: Hdac3 Complexesmentioning

confidence: 94%

“…The role of SMRT/N-CoR extends beyond the recruitment of HDAC3 to specific chromatin loci, since their interaction with HDAC3 strongly potentiates HDAC3 enzymatic activity (Wen et al, 2000;Guenther et al, 2001;Zhang et al, 2002). Guenther et al (2001) mapped a domain highly conserved between N-CoR and SMRT, required for interaction with HDAC3 and activation of its catalytic function.…”

Section: Regulation Of Hdac3 Activitymentioning

confidence: 99%

“…As discussed next, several nonhistone proteins including cytoplasmic proteins have been shown to be deacetylated by this enzyme. Given that proper association with N-CoR/SMRT is required for the enzyme to be functional toward histones (Wen et al, 2000;Guenther et al, 2001;Zhang et al, 2002), an intriguing question is whether a similar mechanism might also be required for an active cytoplasmic HDAC3 and/or toward nonhistone substrates.…”

Section: Regulation Of Hdac3 Activitymentioning

confidence: 99%

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HDAC3: taking the SMRT-N-CoRrect road to repression

2007

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Known histone deacetylases (HDACs) are divided into different classes, and HDAC3 belongs to Class I. Through forming multiprotein complexes with the corepressors SMRT and N-CoR, HDAC3 regulates the transcription of a plethora of genes. A growing list of nonhistone substrates extends the role of HDAC3 beyond transcriptional repression. Here, we review data on the composition, regulation and mechanism of action of the SMRT/ N-CoR-HDAC3 complexes and provide several examples of nontranscriptional functions, to illustrate the wide variety of physiological processes affected by this deacetylase. Furthermore, we discuss the implication of HDAC3 in cancer, focusing on leukemia. We conclude with some thoughts about the potential therapeutic efficacies of HDAC3 activity modulation.

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The histone deacetylase-3 complex contains nuclear receptor corepressors

Cited by 323 publications

References 32 publications

Class II histone deacetylases: versatile regulators

Class II histone deacetylases: versatile regulators

SUMOylation of the Corepressor N-CoR Modulates Its Capacity to Repress Transcription

HDAC3: taking the SMRT-N-CoRrect road to repression

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