Recent insights into Histone Acetyltransferase-1: biological function and involvement in pathogenesis
Open accessAbstract
Acetylation of histone and non-histone proteins is a post-translational modification mostly associated with activation of gene transcription. The first histone acetyltransferase (HAT) identified as modifying newly synthesized histone H4 in yeast was a type B HAT named HAT1. Although it was the first HAT to be discovered, HAT1 remains one of the most poorly studied enzymes in its class. In addition to its well-established role in the cytoplasm, recent findings have revealed new and intriguing aspects of the function of HAT1 in the nucleus. Several studies have described its involvement in regulating different pathways associated with a wide range of diseases, including cancer. This review focuses on our current understanding of HAT1, highlighting its importance in regulating chromatin replication and gene expression. This previously unknown role for HAT1 opens up novel scenarios in which further studies will be required to better understand its function.
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Major HAT families include GNAT, p300/CBP, MYST, and Rtt109.
“Major HAT families include GNAT, p300/CBP, MYST, and Rtt109 (Poziello et al., 2021; Sabnis, 2021; Di Cerbo and Schneider, 2013).”
From Histone modifications and depression: epigenetic mechanisms, therapeutic targets, and translational outlook (2026) · cites this paper as Poziello et al., 2021
The Introduction (page unavailable) identifies GNAT, p300/CBP, and MYST as three main families of mammalian HATs. It does not include Rtt109 in that classification; Rtt109 appears only in a cited reference title. Thus the source supports three of the four families listed, but not the full claim. (LLM, conf=0.88)
Experimental — accuracy not yet measuredAcetylation is catalyzed by histone acetyltransferases, which neutralize lysine residues, loosen DNA-histone interactions, and promote chromatin accessibility.
“Acetylation is catalyzed by histone acetyltransferases (HATs), which neutralize lysine residues, loosen DNA–histone interactions, and promote chromatin accessibility.”
From Histone modifications and depression: epigenetic mechanisms, therapeutic targets, and translational outlook (2026) · cites this paper as Poziello et al., 2021
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JMJD1B, a novel player in histone H3 and H4 processing to ensure genome stability
Saavedra, F., Gurard-Levin, Z. A., Rojas-Villalobos, C., Vassias, I., Quatrini, R., Almouzni, G., & Loyola, A. (2020) · Epigenetics & Chromatin · doi:10.1186/s13072-020-00331-1 · Cited by 19 · see citing works
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Patent Spotlight: small-molecule Lysine Acetyltransferase Inhibitors (KATi)
Brown, J. A. L. (2020) · Pharmaceutical Patent Analyst · doi:10.4155/ppa-2019-0025 · Cited by 12 · see citing works
Flagged first, then by citations
Research works printed but not linked: 1
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Cited by
Sorted by citations
Acetylation of histone H3 in cancer progression and prognosis
Miziak, P., Baran, M., Borkiewicz, L., Trombik, T., & Stepulak, A. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252010982 · Cited by 49 · see citing works
Lv, L.-Z., Wang, Z.-D., Ren, J.-J., Li, L.-H., Liu, X.-B., Li, J.-L., Zhu, H., Jiang, B., Han, Y.-P., Zhou, X.-M., et al. (2026) · Frontiers in Genetics · doi:10.3389/fgene.2025.1722453 · Cited by 7 · see citing works
- Authors
- Poziello, A., Nebbioso, A., Stunnenberg, H. G., Martens, J. H. A., Carafa, V., & Altucci, L.
- Affiliations
- Radboud University Nijmegen (NL)
- University of Campania "Luigi Vanvitelli" (IT)
- Corresponding author
- Altucci, Lucia
- Venue
- Epigenetics
- Publisher
- Informa UK Limited
- Published
- 2020-10-04
- Volume
- 16
- Issue
- 8
- Pages
- 838-850
- ISSN
- 1559-2294 (ISSN-L)
- 1559-2308
- PMC
- PMC8330999
- OpenAlex
- W3091558907
- Cited by
- 44
- References
- 96
- Citations by year
- 2026: 5 · 2025: 10 · 2024: 10 · 2023: 7 · 2022: 11 · 2021: 1
- FWCI
- 0.45
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Epigenetics (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- Archivio Istituzionale della Ricerca - Università degli Studi della Campania "Luigi Vanvitelli" (submittedVersion)
- Radboud Repository (Radboud University) (submittedVersion)
- Funders
- Vanvitelli per la Ricerca: ‘CAMPANIA’ (ID 342)
- AdipCare (ID 263)
- Campania Regional Government Technology Platform Lotta alle Patologie Oncologiche: iCURE (B21C17000030007)
- Campania Regional Government FASE2: IDEAL (B63D18000560007)
- MIUR (POC01_00043)
- AP holds a PhD fellowship (‘B25D18000010006ʹ PON-2017)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Histone Deacetylase Inhibitors Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
- Keywords
- HAT1, histone acetylation, non-histone protein acetylation, histone H4, chromatin replication, gene expression regulation, nuclear function, cancer, epigenetic regulation
- MeSH terms
- Acetylation, Histones, DNA Methylation, Histone Acetyltransferases
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