Double duty: ZMYND8 in the DNA damage response and cancer
Open accessAbstract
Our genetic information is organized into chromatin, which consists of histones and proteins involved in regulating DNA compaction, accessibility and function. Chromatin is decorated by histone modifications, which provide signals that coordinate DNA-based processes including transcription and DNA damage response (DDR) pathways. A major signal involved in these processes is acetylation, which when attached to lysines within proteins, including histones, can be recognized and read by bromodomain-containing proteins. We recently identified the bromodomain protein ZMYND8 (also known as RACK7 and PRKCBP1) as a critical DNA damage response factor involved in regulating transcriptional responses and DNA repair activities at DNA double-strand breaks. Other studies have further defined the molecular details for how ZMYND8 interacts with chromatin and other chromatin modifying proteins to exert its DNA damage response functions. ZMYND8 also plays essential roles in regulating transcription during normal cellular growth, perturbation of which promotes cellular processes involved in cancer initiation and progression. In addition to acetylation, histone methylation and demethylase enzymes have emerged as important regulators of ZMYND8. Here we discuss our current understanding of the molecular mechanisms that govern ZMYND8 function within chromatin, highlighting the importance of this protein for genome maintenance both during the DDR and in cancer.
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ZMYND8 occupies many active enhancers and recruits KDM5C to super enhancer regions to maintain low H3K4me3 levels resulting in repression of enhancer activity.
“ZMYND8 occupies many active enhancers and recruits KDM5C to super enhancer regions to maintain low H3K4me3 levels resulting in the repression of enhancer activity 35–37.”
From HBO1 functions as an epigenetic barrier to hepatocyte plasticity and reprogramming during liver injury (2025) · cites this paper as [35]
ZMYND8 functions as a reader to recognize the acetylation of histone 3 at K14.
“ZMYND8 (also named PRKCBP1 or RACK7) functions as a reader to recognize the acetylation of histone 3 at K14.”
From HBO1 functions as an epigenetic barrier to hepatocyte plasticity and reprogramming during liver injury (2025) · cites this paper as [35]
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Yuan, W.-C., Earl, A. S., Ma, S., Alcedo, K., Russell, J. O., Duarte, F. M., Chu, Y.-T., Chang, P.-C., Chen, H.-Y., Chi, H.-H., et al. (2025) · Cell Stem Cell · doi:10.1016/j.stem.2025.04.010 · Cited by 7 · see citing works
- Authors
- Gong, F., & Miller, K. M.
- Affiliations
- The University of Texas at Austin (US)
- Corresponding author
- Miller, Kyle M.
- Venue
- Cell Cycle
- Publisher
- Informa UK Limited
- Published
- 2018-02-16
- Volume
- 17
- Issue
- 4
- Pages
- 414-420
- ISSN
- 1538-4101 (ISSN-L)
- 1551-4005
- PMC
- PMC5927707
- OpenAlex
- W2794148770
- Cited by
- 36
- References
- 10
- Citations by year
- 2026: 5 · 2025: 5 · 2024: 4 · 2023: 3 · 2022: 4 · 2021: 4 · 2020: 5 · 2019: 6
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Cell Cycle (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- HHS | NIH | National Cancer Institute (NCI)s (CA201268)
- American Cancer Society (RSG-16-042-01-DMC)
- HHS | NIH | National Cancer Institute (CA198279)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chromatin Remodeling and Cancer
- Keywords
- ZMYND8, DNA damage response, DNA double-strand breaks, DNA repair, chromatin, histone acetylation, bromodomain proteins, histone methylation, histone demethylase, transcriptional regulation, genome maintenance, cancer
- MeSH terms
- Chromatin, DNA Repair, Humans, Neoplasm Metastasis, Neoplasms, Protein Processing, Post-Translational, Transcription, Genetic, Signal Transduction, Tumor Suppressor Proteins, DNA Breaks, Double-Stranded, Mi-2 Nucleosome Remodeling and Deacetylase Complex, Retinoblastoma-Binding Protein 2
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