The DOI matches its Crossref record; 10 of the 10 references it cites were found in a registry or an index.
Histone deacetylase (HDAC) 1 and 2 are essential for accurate cell division and the pluripotency of embryonic stem cells
Open accessAbstract
Significance: Histone deacetylase 1 and 2 (HDAC1/2) are sister proteins that regulate access to DNA by modulating chromatin. We have generated the first double knockout (DKO) of Hdac1/2 in embryonic stem (ES) cells and find that gene inactivation causes a loss of cell viability, which is associated with increased abnormal mitotic spindles and chromosome segregation defects. Transcriptome analysis revealed that almost 2,000 genes are deregulated in DKO cells. Significantly for the self-renewal properties of ES cells, this includes down-regulation of the core pluripotent factors, Oct4, Nanog, and Rex1. Furthermore, using the rescue of Hdac1/2 -null cells as a model system to monitor HDAC1/2 activity, we have also shown that mutations that abolish inositol tetraphosphate binding reduce the activity of HDAC1 in vivo.
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Citations
Cites
Lysine acetylation targets protein complexes and co-regulates major cellular functions
Choudhary, C., Kumar, C., Gnad, F., Nielsen, M. L., Rehman, M., Walther, T. C., Olsen, J. V., & Mann, M. (2009) · Science · doi:10.1126/science.1175371 · Cited by 4,040
Histone acetylation in chromatin structure and transcription
Grunstein, M. (1997) · Nature · doi:10.1038/38664 · Cited by 2,884
HDAC2 negatively regulates memory formation and synaptic plasticity
Guan, J.-S., Haggarty, S. J., Giacometti, E., Dannenberg, J.-H., Joseph, N., Gao, J., Nieland, T. J. F., Zhou, Y., Wang, X., Mazitschek, R., et al. (2009) · Nature · doi:10.1038/nature07925 · Cited by 1,644
Genome-wide mapping of HATs and HDACs reveals distinct functions in active and inactive genes
Wang, Z., Zang, C., Cui, K., Schones, D. E., Barski, A., Peng, W., & Zhao, K. (2009) · Cell · doi:10.1016/j.cell.2009.06.049 · Cited by 1,344
Zhang, Y., Ng, H.-H., Erdjument-Bromage, H., Tempst, P., Bird, A., & Reinberg, D. (1999) · Genes & Development · doi:10.1101/gad.13.15.1924 · Cited by 1,103
Fischle, W., Dequiedt, F., Hendzel, M. J., Guenther, M. G., Lazar, M. A., Voelter, W., & Verdin, E. (2002) · Molecular Cell · doi:10.1016/s1097-2765(01)00429-4 · Cited by 754 · cited 1×
“To confirm this, we transfected DKO cells with cDNAs for wild type and a catalytically inactive version [HDAC1 (32)] of HDAC1 to assess their ability to rescue cell viability (Fig.”
MethodStructure of Hdac3 Bound to Co-Repressor and Inositol Tetraphosphate
Watson, P. J., Fairall, L., Santos, G. M., & Schwabe, J. W. R. (2012) · Nature · doi:10.1038/nature10728 · Cited by 505 · cited 1×
“Although it was previously thought that HDAC complexes are constitutively active, it was recently shown that the deacetylase activity of HDAC1 and HDAC3 is regulated through binding of an IP4 molecule sandwiched between the HDAC and its cognate corepressor (5, 43).”
BackgroundSelf-citationRegulatory networks define phenotypic classes of human stem cell lines
Müller, F.-J., Laurent, L. C., Kostka, D., Ulitsky, I., Williams, R., Lu, C., Park, I.-H., Rao, M. S., Shamir, R., Schwartz, P. H., et al. (2008) · Nature · doi:10.1038/nature07213 · Cited by 343 · cited 1×
“Recent bioinformatics analyses have uncovered the “PluriNet,” a common set of characteristics shared by all pluripotent stem cell lines (31).”
BackgroundKelly, R. D. W., & Cowley, S. M. (2013) · Biochemical Society Transactions · doi:10.1042/bst20130010 · Cited by 297
Self-citationGenome-wide binding map of the histone deacetylase Rpd3 in yeast
Kurdistani, S. K., Robyr, D., Tavazoie, S., & Grunstein, M. (2002) · Nature Genetics · doi:10.1038/ng907 · Cited by 279
Cited by
Modulation of cellular processes by histone and non-histone protein acetylation
Shvedunova, M., & Akhtar, A. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-021-00441-y · Cited by 936
Pi, L., Aichinger, E., van der Graaff, E., Llavata-Peris, C. I., Weijers, D., Hennig, L., Groot, E., & Laux, T. (2015) · Developmental Cell · doi:10.1016/j.devcel.2015.04.024 · Cited by 379
Insights into the activation mechanism of class I HDAC complexes by inositol phosphates
Watson, P. J., Millard, C. J., Riley, A. M., Robertson, N. S., Wright, L. C., Godage, H. Y., Cowley, S. M., Jamieson, A. G., Potter, B. V. L., & Schwabe, J. W. R. (2016) · Nature Communications · doi:10.1038/ncomms11262 · Cited by 244
Self-citationKelly, R. D. W., Chandru, A., Watson, P. J., Song, Y., Blades, M., Robertson, N. S., Jamieson, A. G., Schwabe, J. W. R., & Cowley, S. M. (2018) · Scientific Reports · doi:10.1038/s41598-018-32927-9 · Cited by 138
Self-citationPROTAC-mediated degradation of class I histone deacetylase enzymes in corepressor complexes
Smalley, J. P., Adams, G. E., Millard, C. J., Song, Y., Norris, J. K. S., Schwabe, J. W. R., Cowley, S. M., & Hodgkinson, J. T. (2020) · Chemical Communications · doi:10.1039/d0cc01485k · Cited by 121
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Metadata
- Authors
- Jamaladdin, S., Kelly, R. D. W., O’Regan, L., Dovey, O. M., Hodson, G. E., Millard, C. J., Portolano, N., Fry, A. M., Schwabe, J. W. R., & Cowley, S. M.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2014-06-23
- Volume
- 111
- Issue
- 27
- Pages
- 9840-9845
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2136121675
- Cited by
- 166
- References
- 10
- FWCI
- 5.35
- Type
- journal article
- Language
- en
- Open access
- bronze
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- CoChat. (2026). Citation check: Histone deacetylase (HDAC) 1 and 2 are essential for accurate cell division and the pluripotency of embryonic stem cells. https://app.cochat.ai/papers/10.1073/pnas.1321330111
- The paper
- Jamaladdin, S., Kelly, R. D. W., O’Regan, L., Dovey, O. M., Hodson, G. E., Millard, C. J., Portolano, N., Fry, A. M., Schwabe, J. W. R., & Cowley, S. M. (2014). Histone deacetylase (HDAC) 1 and 2 are essential for accurate cell division and the pluripotency of embryonic stem cells. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.1321330111
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
