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Inhibition of PRC2 Activity by a Gain-of-Function H3 Mutation Found in Pediatric Glioblastoma
Open accessAbstract
EZ Inhibition: Missense mutations in the core constituents of the genome packaging material, chromatin, have been implicated in several of human cancers. Nucleosomes are made up of histones, and a mutation of lysine 27 (K27) to methionine in the N-terminal tail of histone variants H3.3 and H3.1 has been identified in various pediatric gliomas. Lewis et al. (p. 857 , published online 28 March; see the Perspective by Morgan and Shilatifard ) show that the polycomb enzyme complex, which can epigenetically modify K27 by addition of a methyl group—and which is often a silencing signal—is itself potently inhibited by replacement of the H3.3/3.1 K27 by methionine. The inhibition of the EZH2 subunit causes an overall reduction of K27 methylation. Methionine mutants of other methylated lysine residues in histone H3 cause similar reductions in methylation levels of the cognate lysine, altering the epigenetic profiles of such cancer cells.
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In the citing paper
“Consequently, tumor cells with the K27M mutation exhibit low levels of H3K27me3 and aberrant gene silencing (4,(7)(8)(9).”
From S -adenosyl methionine is necessary for inhibition of the methyltransferase G9a by the lysine 9 to methionine mutation on histone H3 (2016) · cites this paper as [7]
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“act in a dominant manner to deplete H3K27 methylation by inhibiting PRC2 methyltransferase activity [5, 6]”
From Histone H3 lysine-to-methionine mutants as a paradigm to study chromatin signaling (2014) · cites this paper as [6]
The cited source says what the claim attributes to it.
In the citing paper
“Additional histone H3 lysine-to-methionine mutants possess dominant gain-of-function activities [6]”
From Histone H3 lysine-to-methionine mutants as a paradigm to study chromatin signaling (2014) · cites this paper as [6]
The cited source says what the claim attributes to it.
In the citing paper
“We and others previously showed that K-to-M oncohistones transform the histone H3 proteins into potent inhibitors of specific lysine methyltransferase enzymes (4-7).”
From S -adenosyl methionine is necessary for inhibition of the methyltransferase G9a by the lysine 9 to methionine mutation on histone H3 (2016) · cites this paper as [7]
The cited source says what the claim attributes to it.
In the citing paper
“Previous studies showed that the K27M mutation found in pediatric glioma is sufficient to transform histone H3 into a potent inhibitor of enzymatic activity of PRC2 (4, 5, 7).”
From S -adenosyl methionine is necessary for inhibition of the methyltransferase G9a by the lysine 9 to methionine mutation on histone H3 (2016) · cites this paper as [7]
The cited source says what the claim attributes to it.
In the citing paper
“we previously showed that H3K9M peptides are capable of inhibiting activity of SUV39H1 and G9a, two H3K9-directed methyltransferases, in vitro (7).”
From S -adenosyl methionine is necessary for inhibition of the methyltransferase G9a by the lysine 9 to methionine mutation on histone H3 (2016) · cites this paper as [7]
The cited source says what the claim attributes to it.
In the citing paper
“Previously, we found that only long, unbranched hydrophobic side chains containing methionine (M) and isoleucine (I) at lysine 27 (K27M and K27I) were capable of inhibiting PRC2 in vitro and decreasing H3K27me3 when expressed ectopically in cultured cells (7).”
From S -adenosyl methionine is necessary for inhibition of the methyltransferase G9a by the lysine 9 to methionine mutation on histone H3 (2016) · cites this paper as [7]
In the citing paper
“Despite reports supporting a higher affinity of PRC2 for H3K27M as compared with wild-type H3 108-110 , H3K27M was often inversely correlated with PRC2 occupancy, challenging the idea that H3K27M sequesters PRC2 on chromatin 111,112 .”
From The roles of DNA, RNA and histone methylation in ageing and cancer (2019) · cites this paper as [112]
In the citing paper
“Expression of the histone mutant is accompanied by a reduction in the levels of Polycomb Repressive Complex 2 (PRC2) mediated H3K27 trimethylation (H3K27me3) and this is purported to be a driving event of DIPG oncogenesis4,5.”
From Therapeutic targeting of polycomb and BET bromodomain proteins in diffuse intrinsic pontine gliomas (2017) · cites this paper as [4]
In the citing paper
“Interestingly upon loss of H3K27me3 these nucleosomes acquire H3K27ac resulting in the formation of H3K27M-K27ac heterotypic nucleosomes4 (Figure 1D and Supplementary Fig. 5B–C).”
From Therapeutic targeting of polycomb and BET bromodomain proteins in diffuse intrinsic pontine gliomas (2017) · cites this paper as [4]
In the citing paper
“As shown by our group and others, H3K27M expression is associated with increased levels of H3K27ac4,5 (Fig. 1D).”
From Therapeutic targeting of polycomb and BET bromodomain proteins in diffuse intrinsic pontine gliomas (2017) · cites this paper as [4]
In the citing paper
“Although still functionally active, PRC2 catalytic property toward H3K27M containing nucleosomes is strongly inhibited4.”
From Therapeutic targeting of polycomb and BET bromodomain proteins in diffuse intrinsic pontine gliomas (2017) · cites this paper as [4]
In the citing paper
“Collectively, these results strongly indicate that H3K27M in DIPG cells does not appear to recruit or sequester EZH2 (or in general PRC2), as suggested by other studies4,6,7.”
From Therapeutic targeting of polycomb and BET bromodomain proteins in diffuse intrinsic pontine gliomas (2017) · cites this paper as [4]
In the citing paper
“Attempts to model H3.3K27M-driven HGG formation in vivo via genetic recombination in neural progenitor/stem cells (NPCs) in the postnatal brain failed to demonstrate tumor-driving activity”
From H3.3K27M Cooperates with Trp53 Loss and PDGFRA Gain in Mouse Embryonic Neural Progenitor Cells to Induce Invasive High-Grade Gliomas (2017) · cites this paper as Lewis et al., 2013
In the citing paper
“H3.3K27M has been shown to have gain-of-function activity inhibiting the Polycomb Repressive Complex 2 (PRC2) (Bender et al., 2013; Lewis et al., 2013), which in turn leads to a global reduction in H3K27me3 levels in primary tumors and tumor-derived primary cells.”
From H3.3K27M Cooperates with Trp53 Loss and PDGFRA Gain in Mouse Embryonic Neural Progenitor Cells to Induce Invasive High-Grade Gliomas (2017) · cites this paper as Lewis et al., 2013
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Metadata
- Authors
- Lewis, P. W., Müller, M. M., Koletsky, M. S., Cordero, F., Lin, S., Banaszynski, L. A., Garcia, B. A., Muir, T. W., Becher, O. J., & Allis, C. D.
- Affiliations
- Rockefeller University (US)
- Princeton University (US)
- Duke University (US)
- University of Pennsylvania (US)
- Corresponding author
- Allis, C. David
- ORCID
- Venue
- Science
- Published
- 2013-05-17
- Volume
- 340
- Issue
- 6134
- Pages
- 857-861
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- PMC
- PMC3951439
- OpenAlex
- W1995105508
- Cited by
- 1,345
- References
- 14
- Citations by year
- 2026: 73 · 2025: 82 · 2024: 103 · 2023: 106 · 2022: 103 · 2021: 118 · 2020: 146 · 2019: 112 · 2018: 84 · 2017: 102 · 2016: 90 · 2015: 95 · 2014: 87 · 2013: 40
- FWCI
- 51.21
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Research Portal (King's College London) (submittedVersion)
- Funders
- National Institutes of Health (DP2OD007447)
- National Institute of Mental Health (P50MH096890)
- National Institute of General Medical Sciences (GM040922, R01GM107047, R01GM040922)
- Topics
- Health Sciences › Medicine › Oncology › Glioma Diagnosis and Treatment
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chromatin Remodeling and Cancer
- Keywords
- pediatric glioblastoma, diffuse intrinsic pontine glioma, H3K27M mutation, histone H3.3, H3K27me3, polycomb repressive complex 2, EZH2, histone methylation, gain-of-function mutations, epigenetic regulation
- MeSH terms
- Enhancer of Zeste Homolog 2 Protein, Animals, Brain Neoplasms, Child, Glioblastoma, Histones, Humans, Lysine, Methionine, Methylation, Transgenes, Amino Acid Substitution, Mutation, Missense, Epigenesis, Genetic, Mice, HEK293 Cells, Polycomb Repressive Complex 2
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