HDAC4 in cancer: A multitasking platform to drive not only epigenetic modifications
Open accessAbstract
Controlling access to genomic information and maintaining its stability are key aspects of cell life. Histone acetylation is a reversible epigenetic modification that allows access to DNA and the assembly of protein complexes that regulate mainly transcription but also other activities. Enzymes known as histone deacetylases (HDACs) are involved in the removal of the acetyl-group or in some cases of small hydrophobic moieties from histones but also from the non-histone substrate. The main achievement of HDACs on histones is to repress transcription and promote the formation of more compact chromatin. There are 18 different HDACs encoded in the human genome. Here we will discuss HDAC4, a member of the class IIa family, and its possible contribution to cancer development.
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HDAC4 can function as a platform to coordinate the activity of class I HDACs.
“HDAC4 can function as a platform to coordinate the activity of class I HDACs16.”
From An HDAC4-specific PROTAC degrader achieves radiation sensitization by enhancing ferroptosis in lung cancer (2026) · cites this paper as [16]
HDAC4 has minimal deacetylase enzymatic activity towards acetyl-lysine.
“Despite having minimal deacetylase enzymatic activity towards acetyl-lysine16”
From An HDAC4-specific PROTAC degrader achieves radiation sensitization by enhancing ferroptosis in lung cancer (2026) · cites this paper as [16]
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200 of 218 shown
- Authors
- Cuttini, E., Goi, C., Pellarin, E., Vida, R., & Brancolini, C.
- Affiliations
- University of Udine (IT)
- Corresponding author
- Brancolini, Claudio
- ORCID
- Brancolini, Claudio
- Venue
- Frontiers in Molecular Biosciences
- Publisher
- Frontiers Media SA
- Published
- 2023-01-24
- Volume
- 10
- Pages
- 1116660-1116660
- ISSN
- 2296-889X (ISSN-L)
- PMC
- PMC9902726
- OpenAlex
- W4317820239
- Cited by
- 28
- References
- 230
- Citations by year
- 2026: 4 · 2025: 6 · 2024: 13 · 2023: 5
- FWCI
- 0.74
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Frontiers in Molecular Biosciences (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Institutional Research Information System (University of Udine) (submittedVersion, other-oa)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- Associazione Italiana per la Ricerca sul Cancro (IG 2021)
- Interreg (ITAT1054)
- Topics
- 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
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Keywords
- HDAC4, histone deacetylase, class IIa HDACs, histone acetylation, epigenetic modifications, chromatin condensation, transcriptional repression, carcinogenesis, non-histone substrates
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