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PHF8 mediates histone H4 lysine 20 demethylation events involved in cell cycle progression.
Open accessAbstract
While reversible histone modifications are linked to an ever-expanding range of biological functions, the demethylases for histone H4 lysine 20 and their potential regulatory roles remain unknown. Here we report that the PHD and Jumonji C (JmjC) domain-containing protein, PHF8, while using multiple substrates, including H3K9me1/2 and H3K27me2, also functions as an H4K20me1 demethylase. PHF8 is recruited to promoters by its PHD domain based on interaction with H3K4me2/3 and controls G1-S transition in conjunction with E2F1, HCF-1 (also known as HCFC1) and SET1A (also known as SETD1A), at least in part, by removing the repressive H4K20me1 mark from a subset of E2F1-regulated gene promoters. Phosphorylation-dependent PHF8 dismissal from chromatin in prophase is apparently required for the accumulation of H4K20me1 during early mitosis, which might represent a component of the condensin II loading process. Accordingly, the HEAT repeat clusters in two non-structural maintenance of chromosomes (SMC) condensin II subunits, N-CAPD3 and N-CAPG2 (also known as NCAPD3 and NCAPG2, respectively), are capable of recognizing H4K20me1, and ChIP-Seq analysis demonstrates a significant overlap of condensin II and H4K20me1 sites in mitotic HeLa cells. Thus, the identification and characterization of an H4K20me1 demethylase, PHF8, has revealed an intimate link between this enzyme and two distinct events in cell cycle progression.
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“As we discussed in the Cell Cycle Regulation section, USP7 deubiquitinates and stabilizes PHF8, allowing the latter to upregulate gene targets involved in cell cycle progression, including cyclin A2 (Liu et al., 2010; Wang et al., 2016).”
From USP7 Is a Master Regulator of Genome Stability (2020) · cites this paper as Liu et al., 2010
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Cites
Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources
Huang, D. W., Sherman, B. T., & Lempicki, R. A. (2009) · Nature Protocols · doi:10.1038/nprot.2008.211 · Cited by 35,890
Ultrafast and memory-efficient alignment of short DNA sequences to the human genome.
Langmead, B., Trapnell, C., Pop, M., & Salzberg, S. L. (2009) · Genome Biology · doi:10.1186/gb-2009-10-3-r25 · Cited by 21,849
Model-based Analysis of ChIP-Seq (MACS)
Zhang, Y., Liu, T., Meyer, C. A., Eeckhoute, J., Johnson, D. S., Bernstein, B. E., Nusbaum, C., Myers, R. M., Brown, M., Li, W., et al. (2008) · Genome Biology · doi:10.1186/gb-2008-9-9-r137 · Cited by 18,386
In silico prediction of protein-protein interactions in human macrophages
Souiai, O., Guerfali, F. Z., Miled, S. B., Brun, C., & Benkahla, A. (2014) · BMC Research Notes · doi:10.1186/1756-0500-7-157 · Cited by 10,785
Significance analysis of microarrays applied to the ionizing radiation response
Tusher, V. G., Tibshirani, R., & Chu, G. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.091062498 · Cited by 10,568
The language of covalent histone modifications
Strahl, B. D., & Allis, C. D. (2000) · Nature · doi:10.1038/47412 · Cited by 8,679 · cited 1×
“Similar results were obtained with PHF8 (1-447) (Fig.”
ResultMaere, S., Heymans, K., & Kuiper, M. T. R. (2005) · Computer applications in the biosciences · doi:10.1093/bioinformatics/bti551 · Cited by 4,163
Histone modifications at human enhancers reflect global cell-type-specific gene expression
Heintzman, N. D., Hon, G. C., Hawkins, R. D., Kheradpour, P., Stark, A., Harp, L. F., Ye, Z., Lee, L. K., Stuart, R. K., Ching, C. W., et al. (2009) · Nature · doi:10.1038/nature07829 · Cited by 2,533 · cited 2×
“The great majority of PHF8-bound promoters overlapped with H3K4me3 (6) and H3K4me2 positive promoters, while very few harbored H4K20me1, H3K9me1/2, or H3K27me2 marks (Fig.”
BackgroundResult[9] TM4 Microarray Software Suite
Saeed, A. I., BHAGABATI, N. K., Braisted, J. C., Liang, W. P., Sharov, V., Howe, E., Li, J., Thiagarajan, M., White, J., & Quackenbush, J. F. (2006) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(06)11009-5 · Cited by 1,996
JmjC-domain-containing proteins and histone demethylation
Klose, R. J., Kallin, E. M., & Zhang, Y. (2006) · Nature Reviews Genetics · doi:10.1038/nrg1945 · Cited by 1,290 · cited 1×
“A gradient for eluting trypsin-digested peptides was established with a time-varying solvent mixture ((min, % of solvent A): (15, 95), (50, 60), (70, 30), (75, 5)) and electrosprayed directly into the LTQ-MS inlet (source voltage, 1.”
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Items 301–400 of 450
Angerilli, A., Tait, J., Berges, J., Shcherbakova, I., Pokrovsky, D., Schauer, T., Smialowski, P., Hsam, O., Mentele, E., Nicetto, D., et al. (2023) · Life Science Alliance · doi:10.26508/lsa.202302023 · Cited by 7
“Several reports demonstrate that knockdown of PHF8 predominantly increases H4K20me1 levels at coding regions and reduces gene expression (Liu et al, 2010; Qi et al, 2010; Asensio-Juan et al, 2017), impacting cytoskeleton organization, cell adhesion, and neurite outgrowth (Asensio-Juan et al, 2012).”
DNA polymerase alpha interacts with PrSet7 and mediates H4K20 monomethylation in Drosophila
Sahashi, R., Crevel, G., Pasko, J., Suyari, O., Nagai, R., Saura, M. M., Yamaguchi, M., & Cotterill, S. (2014) · Journal of Cell Science · doi:10.1242/jcs.144501 · Cited by 7
“It could also be mediated by prevention of the removal of H4K20 monomethylation [e.g. by the demethylase PHF8 (Liu et al., 2010) or by conversion to di and tri forms].”
BackgroundMethodCell-cycle regulation of non-enzymatic functions of the Drosophila methyltransferase PR-Set7
Zouaz, A., Fernando, C., Perez, Y., Sardet, C., Julien, E., & Grimaud, C. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky034 · Cited by 7
“Therefore, it has been notably shown that H4K20me1 could promote the recruitment of Cap-D3 and Cap-G2, two other members of condensin II complex (53).”
BackgroundDiscovery and structural studies of histone demethylases
Peng, L., Li, X., Yang, H., Chen, H., Yue, Y., & Peng, S. (2025) · Frontiers in Epigenetics and Epigenomics · doi:10.3389/freae.2025.1594400 · Cited by 6
KDM7 Demethylases: Regulation, Function and Therapeutic Targeting
Shao, P., Liu, Q., & Qi, H. H. (2023) · Advances in experimental medicine and biology · doi:10.1007/978-3-031-38176-8_8 · Cited by 6
Broad histone H4 monomethylation marks expressed genes involved in translation
Fatemiyan, N., & Davie, J. (2023) · Genome · doi:10.1139/gen-2023-0011 · Cited by 6
Compromised Mitotic Fidelity in Human Pluripotent Stem Cells
Milagre, I., Pereira, C. A., & Oliveira, R. A. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241511933 · Cited by 6
“Moreover, impaired recruitment of centromeric [75,76] as well as structural maintenance of chromosomes [77,78], kinases [79] and other proteins [78], to chromosomes, lead to defects in recruiting the downstream effectors of mitosis [80].”
H4K20 monomethylation faces the WNT
Schotta, G. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1100147108 · Cited by 6
“Alternatively, H4K20me1 could be actively removed by histone demethylases (6).”
BackgroundThe emerging roles for histone demethylases in the modulation of signaling pathways
Stefano, L. D., & Dyson, N. J. (2012) · BioMolecular Concepts · doi:10.1515/bmc-2012-0031 · Cited by 6
“The PHF cluster demethylates H3K9me2/me1 and H3K27me2/me1 (58 – 63) , and more recently, KDM7B/PHF8 was shown to demethylate H4K20me1, a mark implicated in cell cycle regulation (64, 65) .”
BAHCC1 binds H4K20me1 to facilitate the MCM complex loading and DNA replication
Li, D., Zhang, Z., Liu, M., Yao, Y., Guo, Y., Mackintosh, S. G., Chen, J., Allison, D. F., Kim, A., Storey, A. J., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-61284-1 · Cited by 5
“BAHCC1, a chromatin-associated factor expressed across almost all cell cycle stages, is particularly enriched in G1/S phase cells and required for ef fi cient execution of DNA replication.”
InfluentialHistone modification cross-talk: analytical tools and molecular mechanisms
Jiang, J., DuBois-Coyne, S. E., Nam, E., Whedon, S. D., Lee, K., & Cole, P. A. (2026) · Biochemical Journal · doi:10.1042/bcj20250115 · Cited by 5
“…B axis; KDM5A demethylase modulating PI3K/AKT/S6K1/PD-L1 signaling; KDM5B/C impacting STING expression [136]), as well as cellular state transitions like epithelial-or endothelial-to-mesenchymal transition (LSD1 demethylase [137]), and cell cycle progression (PHF8 demethylase [138]).”
Functional Characterization of a Phf8 Processed Pseudogene in the Mouse Genome
St-Germain, J., Khan, M. R., Bavykina, V., Desmarais, R., Scott, M., Boissonneault, G., Brunet, M. A., & Laurent, B. (2023) · Genes · doi:10.3390/genes14010172 · Cited by 5
“Through its dynamic modulation of histone methylation, PHF8 participates in cell cycle regulation [30].”
BackgroundInfluentialEpigenetics, MicroRNAs and Human Cancer
Xia, J., Guo, X., & Deng, K. (2014) · Springer eBooks · doi:10.1007/978-3-319-03725-7_2 · Cited by 5
“To date, the members of JMJC family have been found to target Lys4, 9, 27 and 36 on H3 and Lys20 on H4 (Iwase et al. 2007 ; Agger et al. 2007 ; Whetstine et al. 2006 ; Tsukada et al. 2006 ; Liu et al. 2010 ).”
BackgroundChromatin Dynamics During the Cell Cycle
Doenecke, D. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-803395-1.00005-8 · Cited by 5
Biological function and regulation of histone 4 lysine 20 methylation in DNA damage response
Kohi, S. M., Feng, T., Tian, Y., & Zhu, W. (2022) · Genome Instability & Disease · doi:10.1007/s42764-022-00063-4 · Cited by 6
Foutadakis, S., Roupakia, E., Liakopoulos, P., Kolovos, P., & Kolettas, E. (2022) · Cancers · doi:10.3390/cancers14205047 · Cited by 5
“For this study we re-analysed the following publicly available datasets: GSM1517085 (DNaseI-seq_DMSO), GSM1517089 (H3K27ac DMSO ChIP-seq), GSM1517093 (p300 DMSO ChIP-seq), GSM1517095 (p300 TNFα ChIP-seq) [51], GSM604656 (p65 DMSO WT ChIPseq), GSM604658 (p65_TNFα WT ChIP-seq) [59], GSM558469 (E2F1 HeLa ChIP-Seq) [60],…”
MethodInfluentialGungi, A., Saha, S., Pal, M., & Galande, S. (2023) · Life Science Alliance · doi:10.26508/lsa.202201619 · Cited by 5
“This is important to maintain the repressed state of transcription to allow mitosis to move forward and is additionally facilitated by the reduction in the levels of the demethylase PHF8 in the prophase of cell division (Karachentsev et al, 2005; Liu et al, 2010).”
Hu, Y., Mu, H., & Yang, Y. (2021) · PubMed · doi:10.14670/hh-18-349 · Cited by 5
“PHF8 (PHD finger protein 8), a histone demethylase, is responsible for catalyzing the removal of methyl groups from monomethylated and dimethylated H3 lysine 9 (H3K9me1/2), monomethylated histone H4 lysine 20 (H4K20me1) and dimethylated H3 lysine 27 (H3K27me2), serving as a transcription coactivator (Kleine-Kohlbreche…”
BackgroundGarcía, M. A., Fueyo, R., & Martínez‐Balbás, M. A. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-802389-1.00010-1 · Cited by 5
Condensin IDC, DPY-21, and CEC-4 maintain X chromosome repression in C. elegans
Trombley, J., Rakozy, A. I., McClear, C. A., Jash, E., & Csankovszki, G. (2025) · PLoS Genetics · doi:10.1371/journal.pgen.1011247 · Cited by 4
“H4K20me1 patterns are not propagated during DNA replication; in fact, H4K20me1 levels decrease in S phase due to the activity of an H4K20me1 demethylase PHF8 [68].”
Epigenetics: major regulators of embryonic neurogenesis
Shen, T., Ji, F., & Jiao, J. (2015) · 中国科学通报：英文版 · doi:10.1007/s11434-015-0871-3 · Cited by 4
“paid to sites of lysine (K) methylation which include H3K4, H3K9 and H3K27 [101–103].”
BackgroundEpigenetic instability caused by absence of CIZ1 drives transformation during quiescence cycles
Dobbs, O. G., Wilson, R. H. C., Newling, K., Ainscough, J., & Coverley, D. (2023) · BMC Biology · doi:10.1186/s12915-023-01671-6 · Cited by 4
“Normally, dissociation of the demethylase PHF8 leads to emergence of H4K20me1 at mitosis and recruitment of NCAPD3 and NCAPG2 [37], while lack of the mono-methyltransferase SET8 results in mitotic chromosome condensation failure [38].”
BackgroundChromatin and epigenetics in aging biology
Greer, E. L., Lee, S. S., & Prahlad, V. (2025) · Genetics · doi:10.1093/genetics/iyaf055 · Cited by 5
Chatterjee, R., & Chatterjee, P. (2012) · The Nucleus · doi:10.1007/s13237-012-0054-4 · Cited by 4
“Furthermore, the DCC that binds both X chromosomes of hermaphrodites to reduce transcript levels by half resembles the conserved condensin like complex required for both mitotic and meiotic chromosome resolution implying the recruitment of proteins to the new task of regulating gene expression [73].”
BackgroundA Chromatin Switch for Chromosome Condensation
Bilodeau, S., & Côté, J. (2012) · Developmental Cell · doi:10.1016/j.devcel.2012.11.016 · Cited by 4
Peptides Derived from Histone 3 and Modified at Position 18 Inhibit Histone Demethylase KDM6 Enzymes
Jones, S. E., Olsen, L., Dorosz, J., Seger, S. T., Andersson, J., Kristensen, L. H., & Gajhede, M. (2018) · ChemBioChem · doi:10.1002/cbic.201800185 · Cited by 4
Histone Lysine Methylation, Demethylation, and Hormonal Gene Regulation
Huang, Y., Dennehey, B. K., & Shi, X. (2017) · Wiley eBooks · doi:10.1002/9783527697274.ch3 · Cited by 4
Monica, R. D., Buonaiuto, M., Cuomo, M., Costabile, D., Schönauer, C., Catapano, G., Chiariotti, L., & Visconti, R. (2025) · Clinical Epigenetics · doi:10.1186/s13148-025-01980-3 · Cited by 3
“Notably, the enzyme that demethylates H4K20 me1 , PHF8, also demethylates the transcriptionally repressive marks H3K9 me1/2 and H3K27 me2 [16].”
Feng, H., Fu, Y., Cui, Z., Zhou, M., Zhang, L., Gao, Z., Ma, S., & Chen, C. (2023) · British Journal of Haematology · doi:10.1111/bjh.18983 · Cited by 3
Zygotic activation of transposable elements during zebrafish early embryogenesis
Li, B., Li, T., Wang, D., Yang, Y., Tan, P., Wang, Y., Yang, Y.-G., Jia, S., & Au, K. F. (2025) · Nature Communications · doi:10.1038/s41467-025-58863-7 · Cited by 4
“19a), including the important embryonic development genes, e.g., phf8 essential for cell cycle 51 , and e2f4 , a key transcription activator 52 .”
He, J. N., Zheng, Z., Luo, X., Hong, Y., Su, W., & Cai, C. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.566504 · Cited by 3
Ahn, A. R., Karamikheirabad, M., Park, M. S., Zhang, J., Kim, H. S., Jeong, J. S., Kim, K. M., Park, H. S., & Jang, K. Y. (2023) · Diagnostics · doi:10.3390/diagnostics13061149 · Cited by 3
“Plant homeodomain finger protein 8 (PHF8) is a histone demethylase [14] and shown to be involved in cell growth, survival, apoptosis, and the epithelial to mesenchymal transition (EMT) of cancer cells [15–18].”
BackgroundKremp, M., Aberle, T., Sock, E., Bohl, B., Hillgärtner, S., Winkler, J., & Wegner, M. (2024) · Glia · doi:10.1002/glia.24538 · Cited by 3
“Preferred substrates for demethylation are lysine 9 and lysine 27 of histone 3 (H3K9 and H3K27), particularly in the mono and dimethylated state, and lysine 20 of histone 4 (H4K20), mainly in the monomethylated state (Horton et al., 2010; Liu et al., 2010).”
BackgroundHistone Demethylases in Prostate Cancer
Wang, L., Guo, W., Kim, K., Pochampalli, M. R., Hung, C.-L., Izumiya, Y., & Kung, H.-J. (2013) · Cancer drug discovery and develogment/Cancer drug discovery and development · doi:10.1007/978-1-4614-8039-6_15 · Cited by 3
Wang, Y., Xu, C., Zhong, B., Zhan, D., Liu, M., Gao, D., Wang, Y., & Qin, J. (2019) · Journal of Proteome Research · doi:10.1021/acs.jproteome.9b00650 · Cited by 3
The biological functions of lysine methyltransferase PR-SET7
LIANG, X.-Q., Du, Y., Wang, D., & Yang, Y. (2013) · Hereditas (Beijing) · doi:10.3724/sp.j.1005.2013.00241 · Cited by 3
“子II(Condensin II)、致命恶性脑瘤因子 1(Lethal(3) malignant brain tumor-like protein 1, L3MBTL1)、p53 结合蛋白 1(p53 binding protein 1, 53BP1)。Condensin II通过相应亚基识别H4K20me1([19]), 诱导染色质固 缩。L3MBTL1 可通过MBT结构域结合H4K20me1 与H4K20me2([20]), 参与基因转录的抑制和染色体固 缩。53BP1通过tandem tudor结构域与H4K20me1结 合, 参与DNA损伤修复([21])。在H4K20me1 的基础上, H4K20 还可分别由SUV4-2…”
BackgroundInfluentialKaushal, S., Bhattacharya, D., Kumar, S., Herr, W., Dhanjal, J. K., & Minocha, S. (2025) · BMC Genomics · doi:10.1186/s12864-025-11786-5 · Cited by 4
“…link sequence-specific DNA-binding transcription factors with chromatin-modifying enzymes such as histone demethylases (KDM1A [14, 15] and PHF8 [16]), Set1 histone H3 lysine 4 methyltransferases, mixed-lin-eage leukemia (MLL) [17–19], histone acetyltransferase (KAT8 MOF) [20, 21], ubiquitin…”
Histone H4 lysine 20 methylation marks genes dynamically regulated during erythroid maturation
Murphy, K. E., Getman, M. R., Lv, X., Murphy, Z. C., Abid, D., Rahman, N. F., Bulger, M., & Steiner, L. A. (2025) · Epigenetics & Chromatin · doi:10.1186/s13072-025-00609-2 · Cited by 2
“Chromatin readers of H4K20me1, such as L3MBTL1, can compact chromatin and repress transcription [15, 43], and deletion of PHF8 is associated with H4K20me1 gain and transcriptional repression [39].”
Lyu, H., Tan, C., Wu, Y., Larsen, M. E., Yu, Q., Kang, G., Wood, C. E., Tang, S., & Liu, B. (2025) · Cell Death and Disease · doi:10.1038/s41419-025-08115-9 · Cited by 2
“…understanding of the molecular basis of HER3-driven TNBC progression, but they also support the notion that targeting HER3 with a blocking Ab or ADC, inhibition of PHF8, and/or leveraging miRNA replacement therapy may represent promising therapeutic strategies for patients with HER3-driven TNBC.”
Wang, A., Qi, D., Ma, Y., Wang, M., Dong, H., Wang, C., Zhang, Y., Zhang, Z., Li, L., Xu, J. H., et al. (2025) · Molecular Cancer · doi:10.1186/s12943-025-02512-6 · Cited by 2
“Several studies proposed the demethylase activities of KDM7A and KDM7B target multiple histone residues, including H3K9me1/2, H3K27me2, and H4K20me1 [222–224].”
Genome Reorganization during Erythroid Differentiation
Ryzhkova, A. S., & Баттулин, Н. Р. (2021) · Genes · doi:10.3390/genes12071012 · Cited by 2
“Finally, forced expression of Setd8 during S-phase in U2OS cells led to increased binding of CAP-D3 and CAP-G2, two subunits of chromatin compaction factor condensin II, to replicating chromosomes which resulted in aberrant pre-mitotic chromatin [35,38].”
BackgroundNCAPD3 is a prognostic biomarker and is correlated with immune infiltrates in glioma.
Qu, L., Che, H., Zhao, J., Lü, X., Ren, Z., Wu, Y., Liu, Q., & Guan, H. (2024) · PubMed · doi:10.14670/hh-18-736 · Cited by 2
Insights into the Dissociation Process and Binding Pattern of the BRCT7/8-PHF8 Complex
Yuan, L., Liang, X., & He, L. (2024) · ACS Omega · doi:10.1021/acsomega.3c09433 · Cited by 2
Cell-cycle dependent inhibition of BRCA1 signaling by the lysine methyltransferase SET8
Perez, Y., Alhourani, F., Patouillard, J., Ribeyre, C., Larroque, M., Baldin, V., Llères, D., Grimaud, C., & Julien, E. (2025) · Cell Cycle · doi:10.1080/15384101.2025.2508114 · Cited by 2
“The absence of methylation of newly synthetized histone H4 may be related to the higher activity of H4K20 demethylases at the onset of DNA replication, as suggested by previous studies on PHF8 and hHR23 enzymes [15,16].”
DNA Replication and Histone Modification
Kimurâ, H., & Sato, Y. (2016) · Springer eBooks · doi:10.1007/978-4-431-55873-6_19 · Cited by 2
Hsiao, T.-H., Chiu, Y., & Shao, Y. J. (2019) · Translational Cancer Research · doi:10.21037/tcr.2019.07.05 · Cited by 2
“The two genes have been reported with roles in chromosome condensation and mitosis (10,11).”
Background‘Enhancing’ red cell fate through epigenetic mechanisms
Rossmann, M. P., & Zon, L. I. (2021) · Current Opinion in Hematology · doi:10.1097/moh.0000000000000654 · Cited by 2
“5 intronic enhancer, which is associated with an increase of H4K20me1 at nearby nucleosomes and shields SCL/TAL1, but not GATA1 and LDB1 from this enhancer [57].”
BackgroundCrain, A. T., Butler, M. B., Hill, C. A., Huynh, M., McGinty, R. K., & Duronio, R. J. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.03.12.584710 · Cited by 2
“Conversely, H4K20me1 has been implicated in chromatin compaction (Lu et al. 2008) and gene repression (Congdon et al. 2010; Abbas et al. 2010; Liu et al. 2010; Kalakonda et al. 2008), either via its association with the transcriptional repressor L(3)mbt or its localization in inactive regions of…”
BackgroundCondensin I DC , H4K20me1, and perinuclear tethering maintain X chromosome repression in C. elegansPreprint
Trombley, J., Rakozy, A. I., McClear, C. A., Jash, E., & Csankovszki, G. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.04.05.588224 · Cited by 2
DNA G-Quadruplex in NRP1 Promoter Facilitates SARS-CoV-2 Infection
Gong, P., Zhang, R., Xiao, K., Shu, H., Li, X., Fan, H., & Sun, X. S. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25084422 · Cited by 1
“To investigate whether E2F1 directly binds to G4s in the promoter, we downloaded ChIP-seq data from HeLa [21], MCF-7 [22], and LNCaP [23] cells and found an occupancy of E2F1 in the promoter of NRP1 (Figure 6D upper panel).”
MethodCell cycle dynamics regulate H3K27 and H3K9 histone modifications in Drosophila
Nogay, L., Maya, A. V., Heckmann, L., Cardamone, F., Grass, I., Singh, A., Frey, A., Ernst, L., Iovino, N., & Classen, A.-K. (2026) · PLoS Biology · doi:10.1371/journal.pbio.3003371 · Cited by 1
Quantitative Comparison of ChIP-Seq Data Sets Using MAnorm
Shao, Z., & Zhang, Y. (2015) · Translational bioinformatics · doi:10.1007/978-94-017-9927-0_4 · Cited by 1
Impacts of Histone Lysine Methylation on Chromatin
Lanouette, S., Haddad, J. F., Zhang, P., & Couture, J.-F. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-802389-1.00002-2 · Cited by 1
DNA and Histone Modifications in Cancer Therapy
Suzuki, T. (2017) · Cancer drug discovery and develogment/Cancer drug discovery and development · doi:10.1007/978-3-319-59786-7_20 · Cited by 1
Chromatin Dynamics During Entry to Quiescence and Compromised Functionality in Cancer Cells
Dobbs, O. G., & Coverley, D. (2022) · Results and problems in cell differentiation · doi:10.1007/978-3-031-06573-6_9 · Cited by 1
The Histone Demethylase PHF8 and Neural Development*
Guo, X., Shen, Y., Bei, L. I. U., Chang, Y., & Duan, X. (2011) · PROGRESS IN BIOCHEMISTRY AND BIOPHYSICS · doi:10.3724/sp.j.1206.2010.00390 · Cited by 1
Kałużna, S., Nawrocki, M. J., Bryl, R., Stefańska, K., Jemielity, M., Mozdziak, P. E., Nowicki, M. O., & Perek, B. (2020) · Medical Journal of Cell Biology · doi:10.2478/acb-2020-0024 · Cited by 1
“The catalytic role of KDM7 members in the demethylation of repressive histone markers such as H3K9me1 / 2, H3K27me1 / 2, or H4K20me1 is characterized by marked differences in substrate specificity between different enzymes [36,37].”
BackgroundBryl, R., Stefańska, K., Chermuła, B., Stelmach, B., Pieńkowski, W., Kulus, J., Perek, J., Wieczorkiewicz, M., Wąsiatycz, G., Ratajczak, K., et al. (2021) · Medical Journal of Cell Biology · doi:10.2478/acb-2021-0001 · Cited by 1
Biette, K. M., Black, J. C., & Whetstine, J. R. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-801080-8.00019-3 · Cited by 1
Oppikofer, M. (2012) · edoc (University of Basel) · doi:10.5451/unibas-006041367
Condensins, Chromatin Remodeling and Gene Transcription
Wilson, L. O. W., & Mallavialle, A. (2013) · InTech eBooks · doi:10.5772/55732
“Ncapg2 and Ncapd3 were found to recognize mono-methylation of H4K20, inducing condensin II to bind to the DNA whereas di-methylation of the histone was found to lead to dissociation of the complex [51].”
BackgroundLysine Post-Translational Modifications of Saccharomyces Cerevisiae Chromatin Proteins
Edwards, C. R. (2012) · ScholarlyCommons (University of Pennsylvania)
The role of ORC6 in the human cell
Ravasz, M. (2014) · Elektronische Hochschulschriften der LMU München (Ludwig-Maximilians-Universität München) · doi:10.5282/edoc.17580
Identification and characterization of potential target genes of the histone demethylase PTDSR/JMJD6
Berdel, A. L. (2012) · Universitätsbibliothek der FU Berlin Hochschulschriftenstelle u. Dokumentenserver · doi:10.17169/refubium-8232
Kallingappa, P. K. (2013) · Research Commons (University of Waikato)
Coschi, C. H. (2013) · Scholarship@Western (Western University)
Petrova, B., & Haering, C. H. (2011) · ChemBioChem · doi:10.1002/cbic.201100531
Quantitative Proteomics Characterization of Chromatin-Remodeling Complexes in Health and Disease
Lakshminarasimhan, M., & Washburn, M. P. (2013) · Springer eBooks · doi:10.1007/978-1-4614-7931-4_9
Muranko, K. (2014) · Scholarship@Western (Western University)
Targeting Non-Acetylation Histone Erasers
Lu, F., & Zhang, H. (2015) · Royal Society of Chemistry eBooks · doi:10.1039/9781782628484-00168
Development and Evaluation of Chemical Probes for the Study of Histone Demethylases
Marholz, L. J. (2015) · CU Scholar (University of Colorado Boulder)
Walsh, R. M. (2016) · Digital Access to Scholarship at Harvard (DASH) (Harvard University)
Genetic Defects Underlie the Non-syndromic Autosomal Recessive Intellectual Disability (NS-ARID)
Saleha, S., Sajid, M., Zafar, S., & Pervaiz, N. (2017) · Open Life Sciences · doi:10.1515/biol-2017-0020
Mitotic Chromosome Assembly In Vitro: Functional Cross Talk between Nucleosomes and CondensinsPreprint
Shintomi, K., & Hirano, T. (2017) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2017.82.033639
“First, why does condensin I appear to function more efficiently on nucleosomal DNA than on nonnucleosomal DNA? Although early studies proposed the model that the nucleosome itself serves as a “receptor” for targeting condensins to chromatin (Liu et al. 2010; Tada et al. 2011), accumulating lines of recent evidence fro…”
BackgroundResultTranscriptional programs during mammalian cell prolifération
Rib, L. (2016) · IRIS
Liu, Q., Borcherding, N. C., Shao, P., Maina, P. K., Zhang, W., & Qi, H. H. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/682476
“Through RNA-seq and pathway analyses, we found that the transcriptional coactivator role of PHF8 downstream of HER2 signaling is dominant over its corepressor role, consistent with most of the studies (Liu et al, 2010; Qi et al, 2010; Shao et al, 2017; Wang et al, 2016).”
BackgroundResultInfluentialAngerilli, A., Tait, J., Berges, J., Shcherbakova, I., Schauer, T., Smialowski, P., Hsam, O., Mentele, E., Nicetto, D., & Rupp, R. A. W. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.12.01.404053
“However, several studies on PHF8/KDM7B, a JmjC-domain containing histone demethylase with H4K20me1-specificity, have consistently revealed that increased H4K20me1 levels result in reduced gene expression (Asensio-Juan et al, 2017; Liu et al, 2010; Qi et al, 2010).”
BackgroundHe, X., Pan, J., Liu, B., Tan, C., Ruan, Y., & Huang, Y. (2019) · Research Square · doi:10.21203/rs.2.11104/v1
“In addition, JmjC protein regulates cell cycle progression by regulating H4K20 methylation [52].”
BackgroundZhou, P., & Li, Y. (2010) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.5786957.5778055
Treviño, L. S., & Walker, C. L. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-801238-3.95610-1
Gungi, A., Pal, M., Saha, S., & Galande, S. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.06.01.494139
Capasso, M., Lasorsa, V. A., Cimmino, F., Avitabile, M., Cantalupo, S., Montella, A., Angelis, B. D., Morini, M., de Torres, C., Castellano, A., et al. (2023) · doi:10.1158/0008-5472.c.6511801.v1
Association of NCAP family genes with prognosis and immune infiltration of human sarcoma
Jiang, G., Tian, Q., Shi, P., Li, Z., Li, Y., Chen, J., Wang, W., Chen, R., Zhong, H., & Wu, G. (2023) · Aging · doi:10.18632/aging.204683
Context-Dependent Functions of KDM6 Lysine Demethylases in Physiology and Disease
Tayari, M. M., Fang, C., & Ntziachristos, P. (2023) · Advances in experimental medicine and biology · doi:10.1007/978-3-031-38176-8_7
Doi, S., Suzuki, T., Soeda, S., Miyata, N., & Inazu, T. (2024) · Biochemistry and Biophysics Reports · doi:10.1016/j.bbrep.2024.101670
“Liu et al. also demonstrated that PHF8 controls the G1-S transition in conjunction with E2F1, HCF-1, and SET1A [9].”
BackgroundCasanova, A. G. (2021) · theses.fr (ABES) · doi:10.70675/d8dd6376zeb96z4976z8db1z2af5f0408e3b
Dobbs, O. G., Wilson, R. H. C., Newling, K., Ainscough, J., & Coverley, D. (2023) · Figshare · doi:10.6084/m9.figshare.23949840
Dobbs, O. G., Wilson, R. H. C., Newling, K., Ainscough, J., & Coverley, D. (2023) · Figshare · doi:10.6084/m9.figshare.23949834
Dobbs, O. G., Wilson, R. H. C., Newling, K., Ainscough, J., & Coverley, D. (2023) · Figshare · doi:10.6084/m9.figshare.23949828
Yu, L., Ji, T., Liao, W., Xu, Y., Fang, Y., Zhu, Q., Nie, J., & Yang, D. (2023) · Figshare · doi:10.6084/m9.figshare.22624228
Dobbs, O. G., Wilson, R. H. C., Newling, K., Ainscough, J., & Coverley, D. (2023) · Figshare · doi:10.6084/m9.figshare.23949825
Dobbs, O. G., Wilson, R. H. C., Newling, K., Ainscough, J., & Coverley, D. (2023) · Figshare · doi:10.6084/m9.figshare.23949837
Filipowicz, A. R., Chen, Q., & Allard, P. (2024) · Elsevier eBooks · doi:10.1016/b978-0-323-95488-4.00139-x
Tait, J., Marthen, C., Hoelscher, B., Straub, T., & Rupp, R. A. W. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.03.18.644017
Metadata
- Authors
- Liu, W., Tanasa, B., Tyurina, O. V., Zhou, T. Y., Gassmann, R., Liu, W. T., Ohgi, K. A., Benner, C., Garcia-Bassets, I., Aggarwal, A. K., Desai, A., Dorrestein, P. C., Glass, C. K., & Rosenfeld, M. G.
- Affiliations
- Howard Hughes Medical Institute (US)
- University of California San Diego (US)
- Icahn School of Medicine at Mount Sinai (US)
- Corresponding author
- Rosenfeld, Michael G.
- ORCID
- Venue
- Nature
- Published
- 2010-07
- Volume
- 466
- Issue
- 7305
- Pages
- 508-512
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC3059551
- OpenAlex
- W2130239280
- Cited by
- 441
- References
- 43
- Citations by year
- 2026: 10 · 2025: 19 · 2024: 17 · 2023: 39 · 2022: 21 · 2021: 37 · 2020: 16 · 2019: 17 · 2018: 19 · 2017: 35 · 2016: 32 · 2015: 30 · 2014: 33 · 2013: 39 · 2012: 33
- FWCI
- 15.23
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- eScholarship (California Digital Library) (submittedVersion)
- Funders
- U.S. Department of Defense
- Howard Hughes Medical Institute
- National Institutes of Health
- University of California, San Diego
- National Heart, Lung, and Blood Institute (R01HL065445)
- National Cancer Institute (R01CA097134)
- National Institute of Diabetes and Digestive and Kidney Diseases (R01DK039949, R37DK039949, R01DK018477)
- National Institute of Neurological Disorders and Stroke (R01NS034934)
- 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 › Cancer-related gene regulation
- Keywords
- PHF8, H4K20me1, Jumonji C domain, cell cycle progression, G1/S transition, E2F1, HCF-1, SET1A, X-linked intellectual disability, craniofacial development, neuronal survival, histone demethylase, chromatin regulation, zebrafish, promoter recruitment
- MeSH terms
- Adenosine Triphosphatases, Cell Cycle, Cell Line, Chromatin, Chromosomal Proteins, Non-Histone, DNA-Binding Proteins, HeLa Cells, Histones, Humans, Lysine, Methylation, Phosphorylation, Promoter Regions, Genetic, Histone-Lysine N-Methyltransferase, Transcription Factors, Protein Structure, Tertiary, Multiprotein Complexes, Host Cell Factor C1, Histone Demethylases
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