Cited by 613Epigenetics and DNA MethylationGenomics and Chromatin DynamicsChromatin Remodeling and Cancer

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Molecular Mechanisms Directing PRC2 Recruitment and H3K27 Methylation

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Laugesen, Anne, Højfeldt, Jonas Westergaard, Helin, Kristian·2019·Molecular Cell

DOI 10.1016/j.molcel.2019.03.011PMC PMC6452890

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Abstract

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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Background
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Background
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“24,25 EZH2 is the catalytic subunit of PRC2.”
Background
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Background
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Background
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Background
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Background
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Influential
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Influential
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Background
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Low-level repressive histone marks fine-tune gene transcription in neural stem cells
Rajan, A., Anhezini, L., Rives-Quinto, N., Chhabra, J. Y., Neville, M. C., Larson, E. D., Goodwin, S. F., Harrison, M. M., & Lee, C. (2023) · eLife · doi:10.7554/elife.86127 · Cited by 14
“High levels of H3K27me3 are associated with inactive enhancers and the body of repressed genes (Laugesen et al., 2019; Piunti and Shilatifard, 2021).”
BackgroundInfluential
TDP-43 Epigenetic Facets and Their Neurodegenerative Implications
Gimenez, J., Spalloni, A., Cappelli, S., Ciaiola, F., Orlando, V., Buratti, E., & Longone, P. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241813807 · Cited by 15
Role of epigenetic regulatory mechanisms in age‐related bone homeostasis imbalance
Zhong, Y., Zhou, X., Pan, Z., Zhang, J., & Pan, J. (2024) · The FASEB Journal · doi:10.1096/fj.202302665r · Cited by 14
“55,74 Depending on the types of histones and residues, histone methylation affects gene transcription differently by either opening or stabilizing chromatin structure.”
Background
Hypermethylation of CDKN2A CpG island drives resistance to PRC2 inhibitors in SWI/SNF loss-of-function tumors
Wang, X., Wang, Y., Xie, M., Ma, S., Zhang, Y., Wang, L., Ge, Y., Li, G., Zhao, M., Chen, S., et al. (2024) · Cell Death and Disease · doi:10.1038/s41419-024-07109-3 · Cited by 14
“Such reader function is important for both the allosteric activation of PRC2 [3] and the expansion of this suppressive marker along the chromatin template [4].”
A conserved switch to less catalytically active Polycomb repressive complexes in non-dividing cells
McCole, R., Nolan, J., Reck, D. M., Monger, C., Rustichelli, S., Conway, E., Brien, G. L., Wang, C., Deevy, O., Neikes, H. K., et al. (2025) · Cell Reports · doi:10.1016/j.celrep.2024.115192 · Cited by 13
Regulation of Gene Expression and the Elucidative Role of CRISPR-Based Epigenetic Modifiers and CRISPR-Induced Chromosome Conformational Changes
Martella, A., & Fisher, D. I. (2021) · The CRISPR Journal · doi:10.1089/crispr.2020.0108 · Cited by 14
“73,76,77 80 Histone acetyl transferases (HATs) are the writer enzymes that deposit acetylation marks, and histone deacetylases (HDACs) are the eraser enzymes.”
Earliest hepatitis B virus-hepatocyte genome integration: sites, mechanism, and significance in carcinogenesis
Chauhan, R., & Michalak, T. I. (2021) · Hepatoma Research · doi:10.20517/2394-5079.2020.136 · Cited by 14
“In addition, we tracked for CCCTC-binding factor (CTCF) clusters linked to insulator activity, enhancer of zeste homolog 2 (EZH2) sequences playing a main role in methylation by activating methyl groups, and for the presence of DNAase binding regions([93-95]).”
Method
Epigenetic priming as a mechanism of predetermination of spermatogonial stem cell fate
McCarrey, J. R. (2022) · Andrology · doi:10.1111/andr.13332 · Cited by 15
DOT1L inhibitors block abnormal self-renewal induced by cohesin loss
Heimbruch, K. E., Fisher, J. B., Stelloh, C. T., Phillips, E., Reimer, M. H., Wargolet, A. J., Meyer, A. E., Pulakanti, K., Viny, A. D., Loppnow, J. J., et al. (2021) · Scientific Reports · doi:10.1038/s41598-021-86646-9 · Cited by 14
Novel insights into lncRNAs as key regulators of post-translational modifications in cancer: mechanisms and therapeutic potential
Han, Y., Li, S., Oyang, L., Cui, S., Zhang, W., Yang, W., Peng, M., Tan, S., Xia, L., Lin, J., et al. (2025) · Cellular Oncology · doi:10.1007/s13402-025-01086-1 · Cited by 14
“For example, enhancer of zeste homolog 2 (EZH2), a catalytic component of the polycomb repressive complex 2 (PRC2), catalyzes the trimethylation of H3K27, leading to the silencing of tumor suppressor genes and driving cancer progression [ 69].”
Chronic Inflammation Pathway NF-κB Cooperates with Epigenetic Reprogramming to Drive the Malignant Progression of Glioblastoma
Lin, K., Gao, W., Chen, N., Yang, S., Wang, H., Wang, R., Xie, F., Meng, J., Lam, E. W. ‐., Ma, C., et al. (2022) · International Journal of Biological Sciences · doi:10.7150/ijbs.73749 · Cited by 13
“EZH2 is a crucial subunit of the PRC2 and catalyzes H3K27me2/3, which are linked to transcriptional silence [23, 45].”
Background
C-terminal binding protein 2 is a novel tumor suppressor targeting the MYC-IRF4 axis in multiple myeloma
Cheung, C. H. Y., Cheng, C., Leung, K. T., Zhang, C., Ho, C. Y., Luo, X., Kam, A. Y. F., Xia, T., Wan, T. S. K., Pitts, H. A., et al. (2024) · Blood Advances · doi:10.1182/bloodadvances.2023010218 · Cited by 13
The eroding chromatin landscape of aging stem cells
Shi, C., Wang, L., & Sen, P. (2020) · Translational Medicine of Aging · doi:10.1016/j.tma.2020.08.002 · Cited by 14
Lysine demethylase 7a regulates murine anterior-posterior development by modulating the transcription of Hox gene cluster
Higashijima, Y., Nagai, N., Yamamoto, M., Kitazawa, T., Kawamura, Y., Taguchi, A., Nakada, N., Nangaku, M., Furukawa, T., Aburatani, H., et al. (2020) · Communications Biology · doi:10.1038/s42003-020-01456-5 · Cited by 13
Re-expression of miR-200s in claudin‐low mammary tumor cells alters cell shape and reduces proliferation and invasion potentially through modulating other miRNAs and SUZ12 regulated genes
Simpson, K. E., Heumen, G. C.-V., Watson, K. L. M., Roth, M., Martin, C., & Moorehead, R. A. (2021) · Cancer Cell International · doi:10.1186/s12935-021-01784-4 · Cited by 14
Ezh2 harnesses the intranuclear actin cytoskeleton to remodel chromatin in differentiating Th cells
Titelbaum, M., Brant, B., Baumel, D., Burstein-Willensky, A., Perez, S., Barsheshet, Y., & Avni, O. (2021) · iScience · doi:10.1016/j.isci.2021.103093 · Cited by 13
“Ezh2 is histone methyltransferase that preferentially trimethylates histone H3 on lysine 27 (H3K27me3), but additional targets were demonstrated (Laugesen et al., 2019; Margueron and Reinberg, 2010; Schuettengruber et al., 2007), and PcG proteins entail non-catalytic activities as well (Muller and Verrijzer, 2009; Pie…”
Background
AP-1 Mediates Cellular Adaptation and Memory Formation During Therapy ResistancePreprint
Li, J., Ravindran, P. T., O’Farrell, A., Busch, G. T., Boe, R. H., Niu, Z., Woo, S., Dunagin, M. C., Jain, N., Goyal, Y., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.07.25.604999 · Cited by 13
“In those cases, enzymes that read and write such modifications are the key to their epigenetic propagation, such as SUV39H1/2 40 and PRC2 41–43 , respectively.”
Background
Level of Foxp3, DNMTs, methylation of Foxp3 promoter region, and CD4 + CD25 + CD127low regulatory T cells in vulvar lichen sclerosus
Wang, L., Yi, J., Chen, H., Wang, P., & Shen, Y. (2021) · The Kaohsiung Journal of Medical Sciences · doi:10.1002/kjm2.12356 · Cited by 14
“The maintenance and catalysis of DNA methylation is conducted by DNMTs.26 DNMT1 and DNMT3 are the two main members of DNMTs. DNMT1 maintains the methylation through DNA replication and repair, while DNMT3 catalyzes the de novo methylation of CpGs.27 In general, DNMTs regulate the transcription of the target genes and…”
Background
The transcriptional elongation factor CTR9 demarcates PRC2-mediated H3K27me3 domains by altering PRC2 subtype equilibrium
Chan, N. T., Huang, J., Ma, G., Zeng, H., Donahue, K., Wang, Y., Li, L., & Xu, W. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac047 · Cited by 12
“Emerging evidence has shown that the active histone marks inhibit PRC2 activity in transcribed regions (67) and that both H3K4me3 and H3K36me2/3 are inhibitory to PRC2 activity (68,69).”
DNA methylation in human gastric epithelial cells defines regional identity without restricting lineage plasticity
Fritsche, K., Boccellato, F., Schlaermann, P., Koeppel, M., Denecke, C., Link, A., Malfertheiner, P., Gut, I., Meyer, T. F., & Berger, H. (2022) · Clinical Epigenetics · doi:10.1186/s13148-022-01406-4 · Cited by 12
“EZH2 is the functional enzymatic subunit of the polycomb repressive complex 2 (PRC2), which catalyzes the methylation of lysine 27 of histone 3 (H3K27), leading to transcriptional repression [32].”
Background
Controllers of histone methylation-modifying enzymes in gastrointestinal cancers
Li, L., Song, Q., Zhou, J., & Ji, Q. (2024) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2024.116488 · Cited by 13
Nano particle loaded EZH2 inhibitors: Increased efficiency and reduced toxicity for malignant solid tumors
Guo, Y., Huang, J., Meng, L., Yin, Q., Zhang, T., Guo, Z., Tang, Y., Cheng, R., Wang, Y., Peng, Y., et al. (2025) · Journal of Translational Internal Medicine · doi:10.1515/jtim-2025-0020 · Cited by 12
Inhibition of CDK2 reduces EZH2 phosphorylation and reactivates ERα expression in high-grade serous ovarian carcinoma.
Han, Y., Wei, Y., Yao, J., Chu, Y., Li, C.-W., Hsu, J. L., Nie, L., & Hung, M. (2020) · PubMed Central · Cited by 12
Single-molecule imaging of epigenetic complexes in living cells: insights from studies on Polycomb group proteins
Brown, K., Andrianakos, H., Ingersoll, S., & Ren, X. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkab304 · Cited by 14
“PRC2 is the methyltransferase that is responsible for methylation of more than 80% of all histone H3 across the genome (61,66).”
BackgroundInfluential
PR‐DUB safeguards Polycomb repression through H2AK119ub1 restriction
Li, R., Huang, D., Zhao, Y., Yuan, Y., Sun, X., Dai, Z., Huo, D., Liu, X., Helin, K., Li, M. J., et al. (2023) · Cell Proliferation · doi:10.1111/cpr.13457 · Cited by 12
“49,54,55 This sampling module allows PRCs to engage all potential target promoters in the genome while only to achieve stable binding at favourable repressive environment through formation of PcG domain or condensates.”
Background
Current understanding of plant Polycomb group proteins and the repressive histone H3 Lysine 27 trimethylation
Jiao, H., Xie, Y., & Li, Z. (2020) · Biochemical Society Transactions · doi:10.1042/bst20200192 · Cited by 12
EZH2 Dynamically Associates With Non-coding RNAs in Mouse Hearts After Acute Angiotensin II Treatment
Wang, S., Guo, N., Li, S., He, Y. M., Zheng, D., Li, L., & Wang, Z. (2021) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2021.585691 · Cited by 12
Polycomb Factor PHF19 Controls Cell Growth and Differentiation Toward Erythroid Pathway in Chronic Myeloid Leukemia Cells
García-Montolio, M., Ballaré, C., Blanco, E., Gutiérrez, A., Aranda, S., Gómez, A., Kok, C. H., Yeung, D. T. O., Hughes, T. P., Vizán, P., et al. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.655201 · Cited by 12
“SUZ12, and EED), several sub-stoichiometric accessory factors have been described to regulate PRC2 genomic localization and function (Vizan et al., 2015; Laugesen et al., 2019).”
Background
Tyrosine 1–phosphorylated RNA polymerase II transcribes PROMPTs to facilitate proximal promoter pausing and induce global transcriptional repression in response to DNA damagePreprint
Ajit, K., Alagia, A., Burger, K., & Gullerová, M. (2024) · Genome Research · doi:10.1101/gr.278644.123 · Cited by 12
“However, PRC1 can also be recruited to H3K27me3 marks deposited by PRC2 (Laugesen et al. 2019).”
Lactylation-boosted polycomb repression of KLF4 elicits glycolysis in retinoblastoma: A positive feedback circuit between histone modifications
Yang, L., Zuo, S., Jia, R., Gu, X., Liao, Q., Hua, Y., Ge, S., He, M., Fan, J., Tong, X., et al. (2025) · Cancer Letters · doi:10.1016/j.canlet.2025.217804 · Cited by 11
Emerging roles of histone methylation in phytopathogenic fungi
Zhang, Q., & Zeng, T. (2025) · aBIOTECH · doi:10.1007/s42994-025-00223-6 · Cited by 11
“In animals, PRC2, a histone methyltransferase complex (Laugesen et al. 2019), catalyzes H3K27me1, 2, and 3: H3K27me2 and 3 repress gene expression while H3K27me1 promotes gene expression (Jacob and Michaels 2009; Shen et al. 2008).”
AP-1 mediates cellular adaptation and memory formation
Li, J., Ravindran, P. T., O’Farrell, A., Busch, G. T., Boe, R. H., Niu, Z., Woo, S., Dunagin, M. C., Jain, N., Goyal, Y., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-70862-w · Cited by 23
“In those cases, enzymes that read and write such modi ﬁ cations are the key to their epigenetic propagation, such as SUV39H1/2 50 and PRC2 51 – 53 , respectively.”
De Novo Polycomb Recruitment and Repressive Domain Formation
Hernández-Romero, I. A., & Valdés, V. J. (2022) · Epigenomes · doi:10.3390/epigenomes6030025 · Cited by 11
“The functional core of PRC2 contains the embryonic ectoderm development protein (Eed), the retinoblastoma binding protein (RbAp46/48), Suz12, and Ezh1/2 that are responsible for the catalysis of mono-, di-, and trimethylation of histone H3 lysine 27 (H3K27me1/2/3) [4,84].”
BackgroundInfluential
Epigenetic regulation of embryonic ectoderm development in stem cell differentiation and transformation during ontogenesis
Huang, L., Li, F., Ye, L., Yu, F., & Wang, C. (2023) · Cell Proliferation · doi:10.1111/cpr.13413 · Cited by 11
ANGPTL2 ‐mediated epigenetic repression of MHC‐I in tumor cells accelerates tumor immune evasion
Kadomatsu, T., Hara, C., Kurahashi, R., Horiguchi, H., Morinaga, J., Miyata, K., Kurano, S., Kanemaru, H., Fukushima, S., Araki, K., et al. (2023) · Molecular Oncology · doi:10.1002/1878-0261.13490 · Cited by 12
“In tRCC cells, Angptl2 or Itg a 5 deﬁciency did not alter expression levels of Ezh2 , embryonic ectoderm development ( Eed ), and Suz12 , all of which encode core subunits of PRC2 complex [34].”
BackgroundInfluential
The Role of Long Noncoding RNAs in Intestinal Health and Diseases: A Focus on the Intestinal Barrier
Lu, Q., Liang, Y., Meng, X., Zhao, Y., Fan, H., & Hou, S. (2023) · Biomolecules · doi:10.3390/biom13111674 · Cited by 12
“It interacts with polycomb repressive complex 2 (PRC2), a chromatin-associated methyltransferase that catalyzes the methylation of lysine 27 on histone H3 (H3K27), thus regulating the transcriptional silencing of genes of the HOXD locus and other gene loci [29,30].”
Background
TRIM37 interacts with EZH2 to epigenetically suppress PTCH1 and regulate stemness in glioma stem cells through sonic hedgehog pathway
Cai, L., Liu, Y., Li, Y., Liu, B., Cao, Y., Yang, W., Wang, B., & Sun, T. (2024) · Journal of Neuro-Oncology · doi:10.1007/s11060-024-04726-y · Cited by 11
“Enhancer of zeste homolog 2 (EZH2) is a significant epigenetic protein that silences genes by inducing histone methylation, playing a crucial role in the regulation of gene expression and chromatin remodeling [ 11].”
Astrocyte allocation during brain development is controlled by Tcf4-mediated fate restriction
Zhang, Y., Li, D., Cai, Y., Zou, R., Zhang, Y., Deng, X., Wang, Y., Tang, T., Ma, Y., Wu, F., et al. (2024) · The EMBO Journal · doi:10.1038/s44318-024-00218-x · Cited by 11
“Furthermore, they should state limitation of this study.”
VEL-dependent polymerization maintains the chromatin association of Polycomb proteins for the switch to epigenetic silencing
Schulten, A., Jang, G., Payne-Dwyer, A. L., Fiedler, M., Nielsen, M., Mateo‐Bonmatí, E., Bienz, M., Leake, M. C., & Dean, C. (2025) · Molecular Cell · doi:10.1016/j.molcel.2025.08.002 · Cited by 11
“36 Our 37–40 In what has been termed a “responsive model” for targeting Polycomb complexes, Polycomb samples along the chromatin for permissive chromatin states and accumulates at specific sites through positive feedback mechanisms.”
Influential
SlimVar for rapid in vivo single-molecule tracking of chromatin regulators in plants
Payne-Dwyer, A. L., Jang, G., Dean, C., & Leake, M. C. (2025) · Nature Communications · doi:10.1038/s41467-025-63108-8 · Cited by 11
MicroRNA-20a Suppresses Tumor Proliferation and Metastasis in Hepatocellular Carcinoma by Directly Targeting EZH1
Zhang, Q., Deng, X., Tang, X., You, Y., Mei, M., Liu, D., Gui, L., Cai, Y., Xin, X., He, X., et al. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.737986 · Cited by 11
“Enhancer of zeste homologue 1 (EZH1) is a member of the Polycomb group (PcG) protein family that plays a crucial role in gene silencing (9, 10).”
Background
Crosstalk between Noncoding RNAs and the Epigenetics Machinery in Pediatric Tumors and Their Microenvironment
Pathania, A. S. (2023) · Cancers · doi:10.3390/cancers15102833 · Cited by 13
“PRC2 catalyzes mono-, di-, and trimethylation of histone H3 at lysine 27 (H3K27me1/2/3), causing chromatin compaction and transcriptional repression [38].”
Background
Domain cross-talk in regulation of histone modifications: Molecular mechanisms and targeting opportunities
Longbotham, J. E., Zhang, M. Y., & Fujimori, D. G. (2020) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2020.06.001 · Cited by 12
Epigenetic Modulation of Radiation-Induced Diacylglycerol Kinase Alpha Expression Prevents Pro-Fibrotic Fibroblast Response
Liu, C., Tóth, R., Bakr, A., Goyal, A., Islam, M. S., Breuer, K., Mayakonda, A., Lin, Y.-Y., Stepper, P., Jurkowski, T. P., et al. (2021) · Cancers · doi:10.3390/cancers13102455 · Cited by 13
“sion, but it can also interact with other proteins to co‐activate PRC2‐independent gene transcription [17,18].”
Background
Epigenetic regulation of cancer stem cells: Shedding light on the refractory/relapsed cancers
Xu, L., Zhang, J., Sun, J., Hou, K., Yang, C., Guo, Y., Liu, X., Kalvakolanu, D. V., Zhang, L., & Guo, B. (2022) · Biochemical Pharmacology · doi:10.1016/j.bcp.2022.115110 · Cited by 11

Authors: Laugesen, A., Højfeldt, J. W., & Helin, K.
Affiliations: University of Copenhagen (DK)
Corresponding author: Helin, Kristian
ORCID: Laugesen, Anne
Højfeldt, Jonas Westergaard
Helin, Kristian
Venue: Molecular Cell
Publisher: Elsevier BV
Published: 2019-04
Volume: 74
Issue: 1
Pages: 8-18
ISSN: 1097-2765 (ISSN-L)
DOI: 10.1016/j.molcel.2019.03.011
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: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 369 d)
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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Molecular Mechanisms Directing PRC2 Recruitment and H3K27 Methylation

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