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Molecular Mechanisms Directing PRC2 Recruitment and H3K27 Methylation
Open accessAbstract
The polycomb repressive complex 2 (PRC2) is a chromatin-associated methyltransferase catalyzing mono-, di-, and trimethylation of lysine 27 on histone H3 (H3K27). This activity is required for normal organismal development and maintenance of gene expression patterns to uphold cell identity. PRC2 function is often deregulated in disease and is a promising candidate for therapeutic targeting in cancer. In this review, we discuss the molecular mechanisms proposed to take part in modulating PRC2 recruitment and shaping H3K27 methylation patterns across the genome. This includes consideration of factors influencing PRC2 residence time on chromatin and PRC2 catalytic activity with a focus on the mechanisms giving rise to regional preferences and differential deposition of H3K27 methylation. We further discuss existing evidence for functional diversity between distinct subsets of PRC2 complexes with the aim of extracting key concepts and highlighting major open questions toward a more complete understanding of PRC2 function.
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“Within the Polycomb Repressive Complex 2 (PRC2), EZH2 serves as the catalytic subunit responsible for depositing the repressive H3K27me3 mark and silencing target genes (Blackledge et al., 2020; Laugesen et al., 2019).”
From Histone modifications and depression: epigenetic mechanisms, therapeutic targets, and translational outlook (2026) · cites this paper as Laugesen et al., 2019
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Kant, P., Sharma, N., Sabharwal, U., & Pandey, A. (2026) · Journal of Plant Biochemistry and Biotechnology · doi:10.1007/s13562-026-01113-8
“In spite of their different origin, all these non-coding RNAs eventually end up recruiting Polycomb Repressive Complex 2 (PRC2) (Laugesen et al. 2019).”
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Pandita, R., & Lind, E. F. (2026) · Cancers · doi:10.3390/cancers18182985
“PRC2 works as a chromatin repressor, and is a part of the EZH2 complex, which is a key histone methyltransferase [124].”
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Knight, T. A., Mella, J., Chen, D., Ferreira, R. S., Miranda, H. C., & Buchwalter, A. L. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.09.14.750687
“22 48 This analysis revealed that genes upregulated in EMD KOs are strongly enriched for H3K27me3 in normal myotubes (Fig.”
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BindingDB Entry 50019828: Triazole-fused pyrimidines in target-based anticancer drug discovery.
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Metadata
- Authors
- Laugesen, A., Højfeldt, J. W., & Helin, K.
- Affiliations
- University of Copenhagen (DK)
- Corresponding author
- Helin, Kristian
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2019-04
- Volume
- 74
- Issue
- 1
- Pages
- 8-18
- ISSN
- 1097-2765 (ISSN-L)
- PMC
- PMC6452890
- OpenAlex
- W2925415367
- Cited by
- 602
- References
- 105
- Citations by year
- 2026: 60 · 2025: 89 · 2024: 85 · 2023: 83 · 2022: 79 · 2021: 87 · 2020: 83 · 2019: 36
- FWCI
- 6.31
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Molecular Cell (publishedVersion)
- Research at the University of Copenhagen (University of Copenhagen) (publishedVersion, other-oa)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Danmarks Grundforskningsfond (DNRF 82)
- Novo Nordisk Fonden (NNF16OC0023234)
- National Cancer Institute (P30CA008748)
- Topics
- 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
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chromatin Remodeling and Cancer
- Keywords
- polycomb repressive complex 2, H3K27 methylation, histone methyltransferase, gene silencing, cancer therapy targets
- MeSH terms
- Animals, Histones, Humans, Lysine, Methylation, Protein Binding, DNA Methylation, Chromatin Assembly and Disassembly, Polycomb Repressive Complex 2
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