Essential function of histone deacetylase 1 in proliferation control and CDK inhibitor repression
Open accessAbstract
Histone deacetylases (HDACs) modulate chromatin structure and transcription, but little is known about their function in mammalian development. HDAC1 was implicated previously in the repression of genes required for cell proliferation and differentiation. Here we show that targeted disruption of both HDAC1 alleles results in embryonic lethality before E10.5 due to severe proliferation defects and retardation in development. HDAC1-deficient embryonic stem cells show reduced proliferation rates, which correlate with decreased cyclin-associated kinase activities and elevated levels of the cyclin-dependent kinase inhibitors p21(WAF1/CIP1) and p27(KIP1). Similarly, expression of p21 and p27 is up-regulated in HDAC1-null embryos. In addition, loss of HDAC1 leads to significantly reduced overall deacetylase activity, hyperacetylation of a subset of histones H3 and H4 and concomitant changes in other histone modifications. The expression of HDAC2 and HDAC3 is induced in HDAC1-deficient cells, but cannot compensate for loss of the enzyme, suggesting a unique function for HDAC1. Our study provides the first evidence that a histone deacetylase is essential for unrestricted cell proliferation by repressing the expression of selective cell cycle inhibitors.
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A knockout of Hdac1 has been reported, and homozygous embryos died around 9.5 dpc.
“A knockout of Hdac1 has been reported and the homozygous embryos died around 9.5 dpc [21], similar to the time of death observed in MommeD5-/- embryos (Figure 5c).”
From A genome-wide screen for modifiers of transgene variegation identifies genes with critical roles in development (2008) · cites this paper as [21]
Both MommeD5 and MommeD10 genes encode proteins involved in histone modification and chromatin remodeling.
“This is consistent with the fact that both genes encode proteins involved in histone modification and chromatin remodeling [21,23-25,30-33].”
From A genome-wide screen for modifiers of transgene variegation identifies genes with critical roles in development (2008) · cites this paper as [21]
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- Authors
- Lagger, G., O'Carroll, D., Rembold, M., Khier, H., Tischler, J., Weitzer, G., Schuettengruber, B., Hauser, C., Brunmeir, R., Jenuwein, T., & Seiser, C.
- Affiliations
- University of Vienna (AT)
- Vienna Biocenter (AT)
- Corresponding author
- Seiser, Christian
- ORCID
- Venue
- The EMBO Journal
- Published
- 2002-06-03
- Volume
- 21
- Issue
- 11
- Pages
- 2672-2681
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC126040
- OpenAlex
- W1910848366
- Cited by
- 760
- References
- 57
- Citations by year
- 2026: 8 · 2025: 15 · 2024: 14 · 2023: 28 · 2022: 12 · 2021: 22 · 2020: 23 · 2019: 20 · 2018: 18 · 2017: 33 · 2016: 35 · 2015: 39 · 2014: 37 · 2013: 54 · 2012: 48
- FWCI
- 9.39
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The EMBO Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Austrian Science Fund
- 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, cell proliferation, cyclin-dependent kinase inhibitors, p21, p27, embryonic lethality, histone deacetylation, histone hyperacetylation, histone modifications, HDAC2, HDAC3, embryonic stem cells, cell cycle regulation, gene repression
- MeSH terms
- Alleles, Animals, Cell Division, Exons, Histone Deacetylases, Histones, Microscopy, Fluorescence, Models, Genetic, Phenotype, Precipitin Tests, Protein Binding, Time Factors, Blotting, Southern, Blotting, Western, Up-Regulation, Cyclins, In Situ Hybridization, Cell Cycle Proteins, Cyclin-Dependent Kinases, Reverse Transcriptase Polymerase Chain Reaction, In Situ Nick-End Labeling, Tumor Suppressor Proteins, Cyclin-Dependent Kinase Inhibitor p21, Cyclin-Dependent Kinase Inhibitor p27, Mice, Histone Deacetylase 1
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