The physiological roles of histone deacetylase (HDAC) 1 and 2: complex co-stars with multiple leading parts
Abstract
HDACs (histone deacetylases) 1 and 2 are ubiquitous long-lived proteins, which are often found together in three major multiprotein co-repressor complexes: Sin3, NuRD (nucleosome remodelling and deacetylation) and CoREST (co-repressor for element-1-silencing transcription factor). Although there is a burgeoning number of non-histone proteins within the acetylome, these complexes contain multiple DNA/chromatin-recognition motifs, which, in combination with transcription factors, target HDAC1/2 to chromatin. Their physiological roles should therefore be viewed within the framework of chromatin manipulation. Classically, HDACs were thought to be recruited predominantly by transcriptional repressors to facilitate local histone deacetylation and transcriptional repression. More recently, genome-wide assays have mapped HDAC1/2 and their associated proteins to transcriptionally active loci and have provided alternative context-specific functions, whereby their repressive functions are subtly exerted to balance transcriptional activation and repression. With a few significant exceptions (early embryogenesis, brain development), HDAC1 and HDAC2 are functionally redundant. In most mouse knockout studies, deletion of both enzymes is required in order to produce a substantial phenotype. HDAC1/2 activity has been implicated in the development of numerous tissue and cell types, including heart, skin, brain, B-cells and T-cells. A common feature in all HDAC1/2-knockout, -knockdown and small-molecule inhibitor studies is a reduction in cell proliferation. A generic role in cell cycle progression could be exploited in cancer cells, by blocking HDAC1/2 activity with small-molecule inhibitors, making them potentially useful drug targets.
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HDAC1 and HDAC2 form the catalytic core of multiple co-repressor complexes, including Sin3, NuRD, CoREST and MiDAC.
“HDAC1 and HDAC2 (HDAC1/2) are highly related deacetylases that form the catalytic core of multiple co-repressor complexes, including, Sin3, NuRD, CoREST and MiDAC19,20.”
From Histone deacetylase (HDAC) 1 and 2 complexes regulate both histone acetylation and crotonylation in vivo (2018) · cites this paper as [19]
The activity of class-I HDACs in vivo is dependent upon binding to an activating partner as part of a multi-protein complex, as typified by HDAC1/CoREST/LSD1 and HDAC3/SMRT/GPS2/TBL1.
“The activity of class-I HDACs in vivo is dependent upon binding to an activating partner, part of a multi-protein complex19,20, as typified by HDAC1/CoREST/LSD1 and HDAC3/SMRT/GPS2/TBL1.”
From Histone deacetylase (HDAC) 1 and 2 complexes regulate both histone acetylation and crotonylation in vivo (2018) · cites this paper as [19]
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- Authors
- Kelly, R. D. W., & Cowley, S. M.
- Affiliations
- University of Leicester (GB)
- Venue
- Biochemical Society Transactions
- Publisher
- Portland Press Ltd.
- Published
- 2013-05-23
- Volume
- 41
- Issue
- 3
- Pages
- 741-749
- ISSN
- 0300-5127 (ISSN-L)
- 1470-8752
- OpenAlex
- W2071962829
- Semantic Scholar
- 21f432d2cd250d2a585a0680be5b15f6db12576d
- Cited by
- 297
- References
- 71
- Citations by year
- 2026: 3 · 2025: 16 · 2024: 20 · 2023: 22 · 2022: 22 · 2021: 33 · 2020: 23 · 2019: 24 · 2018: 33 · 2017: 22 · 2016: 32 · 2015: 23 · 2014: 21 · 2013: 3
- FWCI
- 2.48
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochemical Society Transactions (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Medical Research Council (MR/J009202/1)
- Biotechnology and Biological Sciences Research Council (BB/J009598/1)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Histone Deacetylase Inhibitors Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
- Keywords
- HDAC1, HDAC2, NuRD complex, CoREST complex, chromatin regulation, transcriptional repression, transcriptional activation, cell proliferation, histone deacetylase inhibitors, cancer drug targets
- MeSH terms
- Acetylation, Animals, Histones, Humans, Models, Biological, Transcription Factors, Signal Transduction, Mice, Knockout, Multiprotein Complexes, Mice, Histone Deacetylase 1, Histone Deacetylase 2, Co-Repressor Proteins
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