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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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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. (2019) · Cancer Research · doi:10.1158/0008-5472.can-19-2883 · Cited by 29
“It is involved in cell-cycle progression where it controls G1–S transition (37).”
BackgroundHow to be a mitotic chromosome
Moser, S. C., & Swedlow, J. R. (2011) · Chromosome Research · doi:10.1007/s10577-011-9198-3 · Cited by 27
“As noted above, the condensin II subunit CAPD3 binds the mono-methylated tail of histone H4 (Liu et al. 2010).”
PHF8-promoted TOPBP1 demethylation drives ATR activation and preserves genome stability
Ma, S., Cao, C., Che, S., Wang, Y., Su, D., Liu, S., Gong, W., Liu, L., Sun, J., Zhao, J., et al. (2021) · Science Advances · doi:10.1126/sciadv.abf7684 · Cited by 29
“As a histone lysine demethylase, plant homeodomain finger protein 8 (PHF8) recognizes lysinemethylated histone H3 lysine 4 (H3K4) with its Nterminal PHD finger and demethylates H3K9me2/ me1, H4K20me1, and H3K27me2 via its Jumonji C (JmjC) domain (27, 28).”
BackgroundKamal, K. Y., Herranz, R., van Loon, J. J. W. A., & Medina, F. J. (2018) · Plant Cell & Environment · doi:10.1111/pce.13422 · Cited by 27
Recognition of methylated histones: new twists and variations
Khorasanizadeh, S. (2011) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2011.10.001 · Cited by 26
Condensin-mediated chromosome organization and gene regulation
Lau, A. C., & Csankovszki, G. (2015) · Frontiers in Genetics · doi:10.3389/fgene.2014.00473 · Cited by 26
“However, it has been shown that mitotic condensin II subunits CAP-D3 and CAP-G2 are capable of binding H4K20me1, suggesting H4K20me1 may play a role in condensin II loading (Liu et al., 2010).”
BackgroundThe histone demethylase PHF8 promotes prostate cancer cell growth by activating the oncomiR miR-125b
Jin, W., Ma, Q., Chen, Z., Jia, G., Lü, X.-Q., & Xie, X. (2015) · OncoTargets and Therapy · doi:10.2147/ott.s85443 · Cited by 26
“Chromatin immunoprecipitation-sequencing data from HeLa cells show that approximately 72% of PHF8-binding sites are at promoters.(5) Also, PHF8 regulates the cell cycle biological processes via removing H4K20me1 from the promoters of certain E2F1-regulated genes.”
Transcriptional regulation of endothelial dysfunction in atherosclerosis: an epigenetic perspective
Xu, Y. (2014) · Journal of Biomedical Research · doi:10.7555/jbr.27.20130055 · Cited by 26
“Several exciting findings have provided clues for such basic biological events as adipogenesis([57]), macrophage activation([58]), and cell cycle progression([59]).”
BackgroundRoles for the methyltransferase SETD8 in DNA damage repair
Xu, L., Zhang, L., Sun, J., Hu, X., Kalvakolanu, D. V., Ren, H., & Guo, B. (2022) · Clinical Epigenetics · doi:10.1186/s13148-022-01251-5 · Cited by 24
Molecular mechanisms of neuroendocrine differentiation in prostate cancer progression
Xie, Y., Ning, S., & Hu, J. (2022) · Journal of Cancer Research and Clinical Oncology · doi:10.1007/s00432-022-04061-7 · Cited by 25
Arteaga, M. F., Mikesch, J.-H., Fung, T.-K., & So, C. W. E. (2014) · British Journal of Cancer · doi:10.1038/bjc.2014.374 · Cited by 25
Shi, G. W., Wu, M., Fang, L., Yu, F., Cheng, S., Li, J., Du, J. X., & Wong, J. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.571653 · Cited by 25
“The enzymatic activity for PHF8 has been extensively studied, and the general conclusion is that PHF8 possesses demethylase activities toward H3K9me1/2 (13, 18, 21–23) and H4K20me1 (23, 24).”
BackgroundRoux, Ö. L., Xie, L., Wang, L., Wu, B., Kong, Q., Wan, Y. Y., & Chen, X. (2016) · Scientific Reports · doi:10.1038/srep24833 · Cited by 25
Wang, W., Sidoli, S., Zhang, W., Wang, Q., Wang, L., Jensen, O. N., Guo, L., Zhao, X., & Zheng, L. (2017) · Scientific Reports · doi:10.1038/srep45103 · Cited by 24
“However, compared to those of the normal glucose condition, Suv4-20h1 , Suv4-20h2 and Phf8 , the genes encoding the key enzymes that regulate H4K20 methylation levels 28 , were not significantly changed after high glucose treatment (Supplementary Fig.”
Cytoskeleton remodeling induced by SMYD2 methyltransferase drives breast cancer metastasis
Casanova, A. G., Roth, G. S., Hausmann, S., Lu, X., Bischoff, L. J. M., Froeliger, E. M., Belmudes, L., a-Flin, E. B., Flores, N. M., Benitez, A. M., et al. (2024) · Cell Discovery · doi:10.1038/s41421-023-00644-x · Cited by 23
“S5a), which shares a high structural redundancy with HEAT repeats 39 known to interact with mono-methylated lysine 20 of H4 40 .”
Kabelitz, T., Brzezinka, K., Friedrich, T., Górka, M., Graf, A., Kappel, C., & Bäurle, I. (2016) · PLANT PHYSIOLOGY · doi:10.1104/pp.15.01688 · Cited by 22
“It is well established for other histone Lys demethylases, such as PHF8, KDM7A, and KDM4, that they have dual specificity depending on the chromatin context and the presence of other binding factors (Klose et al., 2006b; Horton et al., 2010; Lin et al., 2010; Liu et al., 2010b; Yang et al., 2010).”
Controlling the Controllers: Regulation of Histone Methylation by Phosphosignalling
Separovich, R. J., Pang, C. N. I., & Wilkins, M. R. (2020) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2020.08.004 · Cited by 23
Histone lysine methyltransferase SET8 is a novel therapeutic target for cancer treatment
Yang, C., Wang, K., Zhou, Y., & Zhang, S. (2021) · Drug Discovery Today · doi:10.1016/j.drudis.2021.05.004 · Cited by 23
Zhou, L., Ouyang, T., Li, M., Hong, T., Alriashy, M. H. S., Meng, W., & Zhang, N. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.784672 · Cited by 24
The SUV4-20H Histone Methyltransferases in Health and Disease
Gabellini, D., & Pedrotti, S. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23094736 · Cited by 25
Chang, Y., Wu, J., Tong, X.-J., Zhou, J., & Ding, J. (2010) · Biochemical Journal · doi:10.1042/bj20101418 · Cited by 23
Chromatin organization changes during the establishment and maintenance of the postmitotic state
Ma, Y., & Buttitta, L. (2017) · Epigenetics & Chromatin · doi:10.1186/s13072-017-0159-8 · Cited by 22
“In addition the activity of histone modifiers can be regulated in a cell cycledependent manner [9-14].”
BackgroundLinks between genome replication and chromatin landscapes
Sequeira‐Mendes, J., & Gutiérrez, C. (2015) · The Plant Journal · doi:10.1111/tpj.12847 · Cited by 21
“…soon after ORI activation, Set7 is degraded by the proteasome in a PCNA (PROLIFERATING CELL NUCLEAR ANTIGEN)- and Cul (CULLIN)-Ddb1 (DNA DAMAGE BINDING PROTEIN 1)-dependent manner and, as a consequence, the levels of H4K20me1 fall sharply (Oda et al., 2009; Liu et al., 2010; Tardat et al., 2010).”
BackgroundJMJD-1.2/PHF8 controls axon guidance by regulating Hedgehog-like signaling
Riveiro, A. R., Mariani, L. L., Malmberg, E., Amendola, P. G., Peltonen, J., Wong, G., & Salcini, A. E. (2017) · Development · doi:10.1242/dev.142695 · Cited by 22
“While the JmjC domain of PHF8 catalyzes the removal of H3K9me2/me1 and H4K20me1, its PHD finger binds H3K4me3 and contributes to the demethylase activity of the protein at appropriate target sites (Feng et al., 2010; Kleine-Kohlbrecher et al., 2010; Liu et al., 2010).”
BackgroundSpatial Proximity and Similarity of the Epigenetic State of Genome Domains
Khrameeva, E. E., Mironov, A. A., Fedonin, G. G., Khaitovich, P., & Gelfand, M. S. (2012) · PLoS ONE · doi:10.1371/journal.pone.0033947 · Cited by 20
“H4K20me1 with the transcription level [35,36] and several papers demonstrate strong dependency between the H4K20me1 mark and the transcriptional repression [37,38].”
BackgroundSubunits of human condensins are potential therapeutic targets for cancers
Wang, H., Yang, S., Li, G., & Cao, X. (2018) · Cell Division · doi:10.1186/s13008-018-0035-3 · Cited by 21
“Consistent with this, hCAPD3 and hCAPG2 are reported to interact with H4K20me1 histone tails and support specific association between H4K20me1 and condensin II [72].”
McCann, T. S., Sobral, L. M., Self, C., Hsieh, J. C. Y., Sechler, M., & Jedlicka, P. (2019) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2019.1580692 · Cited by 21
Post-transcriptional gene silencing, transcriptional gene silencing and human immunodeficiency virus
Méndez, C. (2015) · World Journal of Virology · doi:10.5501/wjv.v4.i3.219 · Cited by 23
Kagami, Y., & Yoshida, K. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2305-z · Cited by 20
Chen, X. P., Huang, M., Fan, D.-M., He, Y., Zhang, W., Ding, J., Peng, B., Pan, X., Liu, Y., Du, J., et al. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae329 · Cited by 21
Self-citationCK2 kinase-mediated PHF8 phosphorylation controls TopBP1 stability to regulate DNA replication
Feng, H., Lu, J., Song, X., Thongkum, A., Zhang, F., Lou, L., Reizes, O., Almasan, A., & Gong, Z. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa756 · Cited by 20
Jia, Y., Wang, L., Du, J., Wang, M., Shen, H., Liu, Z., Qin, Y., Liu, J., Hu, G.-S., Xiao, R.-Q., et al. (2023) · Developmental Cell · doi:10.1016/j.devcel.2023.03.015 · Cited by 21
Self-citationTargeting the PHF8/YY1 axis suppresses cancer cell growth through modulation of ROS
Wu, X., Li, J.-Y., He, Q., Li, B., He, Y., Pan, X., Wang, M., Sang, R., Ding, J.-C., Gao, X., et al. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2219352120 · Cited by 20
“S8 S and T ), which supports the specificity of iPHF8. iPHF8 treatment led to a significant increase of cellular H3K9me1/2 and H4K20me1 levels, but not H3K4me2, H3K36me3, and H3K79me2 levels (Fig.”
BackgroundSelf-citationHistone demethylase PHF8 regulates hypoxia signaling through HIF1α and H3K4me3
Maina, P. K., Shao, P., Jia, X., Liu, Q., Umesalma, S., Marin, M. J., Long, D., Concepción-Román, S., & Qi, H. H. (2017) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2017.07.005 · Cited by 19
“PHF8 has been reported to interact with components of the H3K4me3 methyltransferase complex, including SETA1 [30] and WDR5 [31], and PHF8 knockdown impairs the recruitment of SETA1 [30].”
BackgroundFu, Y., Yang, Y., Wang, X., Yin, X., Zhou, M., Wang, S., Yang, L. S., Huang, T., Xu, M., & Chen, C. (2018) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2018.01.049 · Cited by 20
Myers, T. R., Amendola, P. G., Lussi, Y., & Salcini, A. E. (2018) · Scientific Reports · doi:10.1038/s41598-018-21914-9 · Cited by 18
The TFIIH complex is required to establish and maintain mitotic chromosome structure
Haase, J., Chen, R., Parker, W. M., Bonner, M. K., Jenkins, L. M., & Kelly, A. E. (2021) · bioRxiv · doi:10.7554/elife.75475 · Cited by 16
A chromatin perspective of plant cell cycle progression
Costas, C., Desvoyes, B., & Gutiérrez, C. (2011) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2011.03.005 · Cited by 21
Kim, H. S., Mukhopadhyay, R., Rothbart, S. B., Silva, A. C., Vanoosthuyse, V., Radovani, E., Kislinger, T., Roguev, A., Ryan, C. J., Xu, J., et al. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.01.029 · Cited by 15
“Z N-terminal tails (Liu et al., 2010; Tada et al., 2011)) and adaptor proteins (e.”
BackgroundTang, W.-S., Weng, L., Wang, X., Liu, C., Hu, G.-S., Yin, S.-T., Ying, T., Hong, N.-N., Guo, H., Liu, W., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109314 · Cited by 19
Self-citationTang, Y., Hong, Y., Bai, H., Wu, Q., Chen, C. D., Lang, J., Boheler, K. R., & Yang, H. (2016) · Stem Cells · doi:10.1002/stem.2333 · Cited by 19
Human 5-lipoxygenase regulates transcription by association to euchromatin
Kreiß, M., Oberlis, J. H., Seuter, S., Bischoff‐Kont, I., Sürün, D., Thomas, D., Göbel, T., Schmid, T., Rådmark, O., Brandes, R. P., et al. (2022) · Biochemical Pharmacology · doi:10.1016/j.bcp.2022.115187 · Cited by 20
“As the identified transcription factors are known chromatin binders [69 – 75], we also included histone marks in the analysis.”
STAG2 Regulates Homologous Recombination Repair and Sensitivity to ATM Inhibition
Zhou, J., Nie, R., He, Z., Cai, X., Chen, J.-W., Lin, W., Yin, Y., Xiang, Z., Zhu, T.-C., Xie, J., et al. (2023) · Advanced Science · doi:10.1002/advs.202302494 · Cited by 18
A Genetic Screen for Functional Partners of Condensin in Fission Yeast
Robellet, X., Fauque, L., Legros, P., Mollereau, E., Janczarski, S., Parrinello, H., Desvignes, J., Thevenin, M., & Bernard, P. (2013) · G3 Genes Genomes Genetics · doi:10.1534/g3.113.009621 · Cited by 18
“Human condensin II binds monomethylated H4-K20 and tends to colocalize with this mark on chromosomes (Liu et al. 2010).”
The histone demethylase PHF8 is a molecular safeguard of the IFNγ response
Asensio-Juan, E., Fueyo, R., Pappa, S., Iacobucci, S., Badosa, C., Lois, S., Balada, M., Bosch‐Presegué, L., Vaquero, A., Gutiérrez, S., et al. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkw1346 · Cited by 18
“PHF8 is the only HDM responsible for demethylating H4K20me1 (17,18).”
BackgroundMethodInfluentialCheng, X., & Trievel, R. C. (2015) · Royal Society of Chemistry eBooks · doi:10.1039/9781782621959-00210 · Cited by 17
An introduction to computational tools for differential binding analysis with ChIP‐seq data
Tu, S., & Shao, Z. (2017) · Quantitative Biology · doi:10.1007/s40484-017-0111-8 · Cited by 17
Nawrocki, M. J., Strugała, A., Piotrowski, P., Wudarski, M., Olesińska, M., & Jagodziński, P. P. (2015) · Zeitschrift für Rheumatologie · doi:10.1007/s00393-015-1619-9 · Cited by 17
Ward, J. R., Khan, A., Torres, S., Crawford, B., Nock, S. L., Frisbie, T. J., Moran, J. V., & Longworth, M. S. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac802 · Cited by 15
“An aliquot of cDNA was generated from 1–2 g of total RNA using the TaqMan Reverse Transcription Reagents (Applied Biosystems) and an oligo-dT(16) primer (Invitrogen).”
MethodCondensins and 3D Organization of the Interphase Nucleus
Wallace, H. A., & Bosco, G. (2013) · Current Genetic Medicine Reports · doi:10.1007/s40142-013-0024-4 · Cited by 16
“raising the possibility that the DCC might bind directly to H4K20me1 to affect compaction of chromatin [92].”
BackgroundPHF8 and REST/NRSF co-occupy gene promoters to regulate proximal gene expression
Wang, J., Lin, X., Wang, S., Wang, C., Wang, Q., Duan, X., Lu, P., Wang, Q., Wang, C., Liu, X., et al. (2014) · Scientific Reports · doi:10.1038/srep05008 · Cited by 16
Genome maintenance in the context of 4D chromatin condensation
Yu, S., Yang, F., & Shen, W. H. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2221-2 · Cited by 17
“Moreover, condensin can recognize and bind monomethylated H4K20, inducing compaction, while dimethylated H4K20 disrupts condensin association to DNA, and consequently leads to decondensation [145].”
One, Two, Three: How Histone Methylation is Read
Fischle, W. (2012) · Epigenomics · doi:10.2217/epi.12.56 · Cited by 16
Mechanisms of Histone Modifications
Vanzan, L., Sklias, A., Bošković, M., Herceg, Z., Murr, R., & Suter, D. M. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-91909-8.00019-0 · Cited by 17
Brénachot, X., Rigault, C., Nédélec, E., Laderrière, A., Khanam, T., Gouazé, A., Chaudy, S., Lemoine, A., Datiche, F., Gascuel, J., et al. (2014) · Molecular Metabolism · doi:10.1016/j.molmet.2014.05.006 · Cited by 15
Zhang, H., Liu, J., He, Y., Xie, Z.-X., Zhang, S., Zhang, Y., Lin, L., Liu, S., & Wang, D. (2019) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2019.04.216 · Cited by 15
Blair, L. P., Avaritt, N. L., Huang, R., Cole, P. A., Taverna, S. D., & Tackett, A. J. (2011) · Epigenetics · doi:10.4161/epi.6.4.14531 · Cited by 14
Jumonji family histone demethylases in neural development
Fueyo, R., García, M. A., & Martínez‐Balbás, M. A. (2014) · Cell and Tissue Research · doi:10.1007/s00441-014-1924-7 · Cited by 15
“…and H3K27me2/1 (Horton et al. 2010; Huang et al. 2010b; Tsukada et al. 2010); PHF8, which demethylates H3K9me2/me1 and H4K20me1 (Horton et al. 2010; Liu et al. 2010; Loenarz et al. 2010; Qi et al. 2010); and PHF2, which targets H3K9me2/me1 and H4K20me3 (Wen et al. 2010; Baba et al. 2011; Stender…”
The histone H4 lysine 20 demethylase DPY-21 regulates the dynamics of condensin DC binding
Breimann, L., Morao, A. K., Kim, J., Jimenez, D. S., Maryn, N., Bikkasani, K., Carrozza, M. J., Albritton, S. E., Kramer, M., Street, L. A., et al. (2021) · Journal of Cell Science · doi:10.1242/jcs.258818 · Cited by 11
Double-strand breaks and the concept of short- and long-term epigenetic memory
Orlowski, C., Mah, L.-J., Vasireddy, R. S., El‐Osta, A., & Karagiannis, T. C. (2010) · Chromosoma · doi:10.1007/s00412-010-0305-6 · Cited by 16
“While PHF8 was recently identified as having H4K20me1 demethylase activity and is involved in cell cycle progression, its role, if any, in regulating DDRspecific H4K20 methylation is unknown (Liu et al. 2010).”
BackgroundFan, T., Xie, J., Huang, G. C., Li, L., Zeng, X., & Tao, Q. (2024) · Epigenomes · doi:10.3390/epigenomes8030036 · Cited by 13
“…localized at the transcription start site (TSS) and acts on the following histone lysine sites: H3K9me1/2, H3K27me2, H4K20me1, and H3K36me2 [35,41], which upon the initiation of PHF8 demethylase activity cause varying degrees of histone demethylation and lead to PHF8-associated…”
BackgroundHistone Methylation in Myelodysplastic Syndromes
Wei, Y., Gañán‐Gómez, I., Dimicoli, S., McCay, S., & Garcia‐Manero, G. (2011) · Epigenomics · doi:10.2217/epi.11.9 · Cited by 13
He, X., Pan, J., Liu, B., Tan, C., Ruan, Y., & Huang, Y. (2021) · PeerJ · doi:10.7717/peerj.11137 · Cited by 14
Introduction—Epiphanies in Epigenetics
Cheng, X., & Blumenthal, R. (2011) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-387685-0.00001-9 · Cited by 14
“44, 45”
Histone modification profiles characterize function-specific gene regulation
Jung, I., & Kim, D. (2012) · Journal of Theoretical Biology · doi:10.1016/j.jtbi.2012.06.009 · Cited by 13
Marshall, A. E., Ishak, C. A., & Dick, F. A. (2019) · Molecular and Cellular Biology · doi:10.1128/mcb.00452-19 · Cited by 13
“condensin II have utilized cell lines that are transformed by viral oncogenes that target RB (13, 42).”
BackgroundComparative distributions of RSBN1 and methylated histone H4 Lysine 20 in the mouse spermatogenesis
Wang, Y., Iwamori, T., Kaneko, T., Iida, H., & Iwamori, N. (2021) · PLoS ONE · doi:10.1371/journal.pone.0253897 · Cited by 13
Development of Substrate-Selective Probes for Affinity Pulldown of Histone Demethylases
Marholz, L. J., Chang, L., Old, W. M., & Wang, X. (2014) · ACS Chemical Biology · doi:10.1021/cb5006867 · Cited by 13
The histone demethylase PHF8 regulates astrocyte differentiation and function
Iacobucci, S., Padilla, N., Gabrielli, M., Navarro, C., Lombardi, M., Vicioso‐Mantis, M., Verderio, C., de la Cruz, X., & Martínez‐Balbás, M. A. (2021) · Development · doi:10.1242/dev.194951 · Cited by 12
SMYD5 acts as a potential biomarker for hepatocellular carcinoma
Chi, G., Pei, J., Li, X., Li, X., Pang, H., Cui, J., Wu, D., Qu, G., & He, Y. (2022) · Experimental Cell Research · doi:10.1016/j.yexcr.2022.113076 · Cited by 12
Roy, A., Niharika, N., Chakraborty, S., Mishra, J., Singh, S. P., & Patra, S. K. (2023) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2023.01.011 · Cited by 11
Lu, T., Yang, J., Cai, Y., Ding, M., Yu, Z., Fang, X., Zhou, X., & Wang, X. (2024) · Journal of Advanced Research · doi:10.1016/j.jare.2024.02.024 · Cited by 12
Current advances and future directions in targeting histone demethylases for cancer therapy
Shin, J.-H., Yoo, H.-B., & Roe, J. (2025) · Molecules and Cells · doi:10.1016/j.mocell.2025.100192 · Cited by 12
The chemistry and biology of the α-ketoglutarate-dependent histone N ε -methyl-lysine demethylases
Zheng, W., & Huang, Y. (2014) · MedChemComm · doi:10.1039/c3md00325f · Cited by 11
Determinants of Human Cyclin B1 Association with Mitotic Chromosomes
Pfaff, K. L., & King, R. W. (2013) · PLoS ONE · doi:10.1371/journal.pone.0059169 · Cited by 11
“lated histone H4K20 that promotes condensin binding [19].”
BackgroundArtificial generation of centromeres and kinetochores to understand their structure and function
Hori, T., & Fukagawa, T. (2020) · Experimental Cell Research · doi:10.1016/j.yexcr.2020.111898 · Cited by 11
Dynamic Control of Chromosome Topology and Gene Expression by a Chromatin ModificationPreprint
Bian, Q., Anderson, E. C., Brejc, K., & Meyer, B. J. (2017) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2017.82.034439 · Cited by 11
“[PubMed: 21363964] Qi HH, Sarkissian M, Hu GQ, Wang Z, Bhattacharjee A, Gordon DB, Gonzales M, Lan F, Ongusaha PP, Huarte M, et al. Histone H4K20/H3K9 demethylase PHF8 regulates zebrafish brain and craniofacial development.”
InfluentialLi, W., Chen, Y.-C., Lin, Y., Zou, Y.-Q., Hu, G.-S., Yang, J.-J., Nie, X. Y., Li, M.-Y., Wang, Y., He, Y., et al. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.115487 · Cited by 12
Self-citationRegulatory mechanism of androgen receptor on NCAPD3 gene expression in prostate cancer
Yin, Y., Liu, Q., Shao, Y., He, X., Zhu, Q., Lu, S., & Liu, P. (2021) · The Prostate · doi:10.1002/pros.24245 · Cited by 10
Chromatin dynamics from S-phase to mitosis: contributions of histone modifications
Doenecke, D. (2014) · Cell and Tissue Research · doi:10.1007/s00441-014-1873-1 · Cited by 10
Dorosz, J., Olsen, L., Seger, S. T., Steinhauer, C., Bouras, G., Helgstrand, C., Wiuf, A., & Gajhede, M. (2017) · ChemBioChem · doi:10.1002/cbic.201700109 · Cited by 10
Downregulation of lncRNA FGF12-AS2 suppresses the tumorigenesis of NSCLC via sponging miR-188-3p
Zhou, L., Chen, X., Zhou, D., Yang, R., & Cai, M. (2020) · Open Medicine · doi:10.1515/med-2020-0219 · Cited by 10
Benefits and pitfalls: Epigenetic modulators in prostate cancer intervention
Upadhyay, N., Tilekar, K. N., Hess, J. D., Pokrovsky, V. S., Aguilera, R. J., & Ramaa, C. S. (2021) · Current Research in Chemical Biology · doi:10.1016/j.crchbi.2021.100006 · Cited by 11
Wang, Y., Wu, L., & Yuen, K. W. Y. (2022) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2022.01.004 · Cited by 10
Yu, L., Ji, T., Liao, W., Xu, Y., Fang, Y., Zhu, Q., Nie, J., & Yang, D. (2023) · Clinical Epigenetics · doi:10.1186/s13148-023-01460-6 · Cited by 10
The Molecular Basis of Histone Demethylation
Horton, J. R., Gale, M., Yan, Q., & Cheng, X. (2017) · Cancer drug discovery and develogment/Cancer drug discovery and development · doi:10.1007/978-3-319-59786-7_7 · Cited by 10
The Role of Histone Methylation and Methyltransferases in Gene Regulation
Cui, J. Y., Fu, Z. D., & Dempsey, J. L. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-812433-8.00002-2 · Cited by 11
Taking Me away: the function of phosphorylation on histone lysine demethylases
Karakatsanis, N. M., Hamey, J. J., & Wilkins, M. R. (2024) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2023.12.004 · Cited by 9
Histone Methylation in Chromatin Signaling
Gozani, O., & Shi, Y. (2013) · Springer eBooks · doi:10.1007/978-1-4614-8624-4_5 · Cited by 8
du Preez, L. L., & Patterton, H. (2017) · Journal of Molecular Modeling · doi:10.1007/s00894-017-3308-x · Cited by 9
“For example, the TAF3-PHD finger recognizes and binds K4Me3 [55, 56], SIRT6 deacetylates K9ac [57], LSD1 demethylates K9Me2 [58], MKP-1 dephosphorylates S10, and PHF8 demethylates both K9Me1/2 and K27Me2 [59].”
BackgroundIn Vitro Histone Demethylase Assays
Kokura, K., Sun, L., & Fang, J. (2015) · Methods in molecular biology · doi:10.1007/978-1-4939-2474-5_8 · Cited by 9
Bookmarking by histone methylation ensures chromosomal integrity during mitosis
Kim, J. (2019) · Archives of Pharmacal Research · doi:10.1007/s12272-019-01156-7 · Cited by 9
“In addition, phosphorylated PHF8 mediated by CDK1/cyclin B1 during prophase dissociates from chromosomes and allows formation of H4K20me1 at early mitosis (Liu et al. 2010).”
BackgroundInfluentialCrain, A. T., Butler, M. B., Hill, C. A., Huynh, M., McGinty, R. K., & Duronio, R. J. (2024) · Genes & Development · doi:10.1101/gad.351698.124 · Cited by 9
“…has been implicated in chromatin compaction (Lu et al. 2008) and gene repression (Kalakonda et al. 2008; Abbas et al. 2010; Congdon et al. 2010; Liu et al. 2010) via either its association with the transcriptional repressor L(3)mbt or its localization in inactive regions of the genome…”
Histone lysine methylation modifiers controlled by protein stability
Park, S., Cho, J. H., Kim, J., & Kim, J. (2024) · Experimental & Molecular Medicine · doi:10.1038/s12276-024-01329-5 · Cited by 9
Fumero, E. F., Walter, C., Frenz, J. M., Seifert, F., Alla, V., Hennig, T., Angenendt, L., Hartmann, W., Wolf, S., Serve, H. L., et al. (2024) · Blood · doi:10.1182/blood.2023021640 · Cited by 8
Schwämmle, V., & Jensen, O. N. (2013) · PLoS ONE · doi:10.1371/journal.pone.0073818 · Cited by 8
Leisegang, M. S., Gu, L., Preussner, J., Günther, S., Hitzel, J., Rațiu, C., Weigert, A., Chen, W., Schwarz, E. C., Looso, M., et al. (2019) · FEBS Letters · doi:10.1002/1873-3468.13337 · Cited by 8
Disrupting PHF8-TOPBP1 connection elicits a breast tumor-specific vulnerability to chemotherapeutics
Ma, S., Zhang, J., Guo, Q., Cao, C., Bao, K., Liu, L., Chen, C. D., Liu, Z., Yang, J., Yang, N., et al. (2022) · Cancer Letters · doi:10.1016/j.canlet.2022.01.010 · Cited by 8
1.4.3 The vector meson nonet (1- states)
Castro-Melchor, M., Le, H., & Hu, W. (2005) · Springer eBooks · doi:10.1007/10201111_6 · Cited by 8
Separovich, R. J., Wong, M. W. M., Bartolec, T. K., Hamey, J. J., & Wilkins, M. R. (2022) · Journal of Molecular Biology · doi:10.1016/j.jmb.2022.167500 · Cited by 7
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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