Cited by 374DNA Repair MechanismsChromatin Remodeling and CancerGenomics and Chromatin Dynamics

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Regulation of DNA‐damage responses and cell‐cycle progression by the chromatin remodelling factor CHD4

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Polo, Sophie E, Kaidi, Abderrahmane, Baskcomb, Linda, Galanty, Yaron, Jackson, Stephen P·2010·The EMBO Journal

DOI 10.1038/emboj.2010.188PMC PMC2944064

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Abstract

The chromatin remodelling factor chromodomain helicase DNA‐binding protein 4 (CHD4) is a catalytic subunit of the NuRD transcriptional repressor complex. Here, we reveal novel functions for CHD4 in the DNA‐damage response (DDR) and cell‐cycle control. We show that CHD4 mediates rapid poly(ADP‐ribose)‐dependent recruitment of the NuRD complex to DNA‐damage sites, and we identify CHD4 as a phosphorylation target for the apical DDR kinase ataxia‐telangiectasia mutated. Functionally, we show that CHD4 promotes repair of DNA double‐strand breaks and cell survival after DNA damage. In addition, we show that CHD4 acts as an important regulator of the G1/S cell‐cycle transition by controlling p53 deacetylation. These results provide new insights into how the chromatin remodelling complex NuRD contributes to maintaining genome stability. This paper adds to the emerging concept that chromatin remodelling contributes to DNA‐damage responses. CHD4, a known NuRD component, is identified as ATM target, localizes to DNA breaks and contributes to repair while associating with PARPylated factors.

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Figure 1 CHD4 is recruited to sites of laser-induced DNA damage within the NuRD complex. (A) Immunodetection of CHD4 and γH2AX (damage sites) at the indicated times after laser micro-irradiation in U2OS cells. (B) Recruitment of NuRD complex subunits to sites of laser-induced DNA damage (labelled by γH2AX) 5 min after micro-irradiation in U2OS cells. (C, D) Immunodetection of HDAC1 and CHD4 5 min after laser micro-irradiation in U2OS cells treated with the indicated siRNAs (siLuci: control). Cells were pre-treated with ATM inhibitor to facilitate detection of HDAC1 and CHD4 lines. Lower panels show siRNA efficiency. In laser micro-irradiation experiments, detergent pre-extraction was performed before fixation of the cells for immunostaining. Scale bars, 10 μm.CC BY-NC-SA · PubMed Central

Figure 2 PARP-dependent recruitment of CHD4 to sites of DNA damage. (A) Immunodetection of CHD4 and γH2AX (damage sites) at the indicated times after laser micro-irradiation in U2OS (left) and A-T cells (right). Cells were pre-incubated for 1 h with the indicated inhibitors (ATMi, ATM inhibitor; PARPi, PARP inhibitor) before micro-irradiation. (B) PAR-binding assay with immunoprecipitated GFP-CHD4 wild-type (WT: residues 1–1937) or truncated mutants (N: residues 1–758; C: residues 1183–1937). GFP only is used as a negative control and GFP-APLF as a positive control. Right panel: corresponding Ponceau staining of the blot after immunoprecipitation from HEK-293 cells. (C) Recruitment of GFP-CHD4 wild-type (WT) or a truncated mutant (C: residues 1183–1937) to sites of laser-induced damage (γH2AX) 5 min after micro-irradiation in U2OS cells. In all cases, detergent pre-extraction was performed before fixation of the cells for immunostaining. Scale bars, 10 μm.CC BY-NC-SA · PubMed Central

Figure 3 ATM-dependent phosphorylation of CHD4 Ser-1346 in response to DNA damage. (A) Detection of CHD4 phosphorylation (αphos-Ab) 1 h after exposure to 10 Gy ionizing radiation (+ IR) on HA immunoprecipitates from U2OS cells transiently expressing HA-CHD4 wild-type (WT) or S1346A point mutant (SA). The scheme represents CHD4 protein with the amino-acid position of the candidate phospho-serine (S1346); the N and C fragments correspond to CHD4 truncated mutants analysed in Figures 2 and 4. Domain organization of CHD4: NLS (putative nuclear localization signal), PHD (plant homeodomain), CHROMO (chromodomain), DEXH (ATP-binding domain), HELIC (helicase carboxyl-terminal domain). (B) Detection of CHD4 S1346 phosphorylation (αphos-Ab) 30 min after cell exposure to 10 Gy ionizing radiation (IR) on HA immunoprecipitates from U2OS cells transiently expressing HA-CHD4. Cells were pre-treated with the indicated inhibitors (W, Wortmannin; PKi, DNA-PK inhibitor; ATMi, ATM inhibitor). ATM-dependent phosphorylation of SMC1 S966 and DNA-PKcs autophosphorylation on S2056 are used as controls.CC BY-NC-SA · PubMed Central

Figure 4 DNA-damage-induced phosphorylation and recruitment of CHD4 to DNA lesions are distinct events. (A) Recruitment of HA-CHD4 wild-type (WT) and Ser-1346 point mutants (SA, mutated to Ala; SE, mutated to Glu) to sites of laser-induced damage (γH2AX) in transiently transfected U2OS cells 5 min after micro-irradiation. Scale bar, 10 μm. (B) PAR-binding activity of GFP-CHD4 from HEK-293 cells exposed or not to ionizing radiation (IR). GFP only is used as a negative control, GFP-APLF as a positive control. Lower panel shows CHD4 phosphorylation after IR analysed in parallel by western blotting. (C) Detection of CHD4 phosphorylation (αphos-Ab) 30 min after exposure to 10 Gy ionizing radiation (IR) or 500 μM hydrogen peroxide (H2O2) on CHD4 immunoprecipitates from HEK-293 cells treated or not with PARP inhibitor (PARPi). SMC1 phosphorylation is used as a control for DNA damage. The NuRD subunit HDAC1 co-immunoprecipitates with CHD4. (D) Detection of CHD4 phosphorylation (αphos-Ab) 30 min after exposure to 10 Gy ionizing radiation (IR) on GFP immunoprecipitates from H3K293 cells transiently expressing GFP-CHD4 wild-type (WT) or a truncated mutant (C: residues 1183–1937).CC BY-NC-SA · PubMed Central

Figure 5 CHD4 regulates cell sensitivity to DNA damage. (A) γH2AX foci formation in U2OS cells upon CHD4 depletion (siCHD4) compared with control (siLuci) 1 h after exposure to 10 Gy ionizing radiation (IR). (B) Phosphorylation of DNA-damage checkpoint proteins analysed by western blotting of total extracts prepared from HeLa cells at the indicated times after cell exposure to 10 Gy ionizing radiation (IR) (siCHD4, CHD4 depletion; siLuci, control). (C) Recruitment of MDC1, 53BP1 and BRCA1 to sites of laser-induced damage (γH2AX) 5–10 min after micro-irradiation in HeLa cells upon CHD4 depletion (siCHD4) compared with control (siLuci). Detergent pre-extraction was performed before fixation and immunostaining for BRCA1. Scale bars, 10 μm. (D) Efficiency of DSB repair in control (siLuci) or CHD4-depleted U2OS cells analysed by neutral comet assay after phleomycin treatment (Phleo). Error bars: s.d. from two independent experiments. (E) Clonogenic survival of U2OS cells upon CHD4 knock-down (siCHD4) compared with control (siLuci) in response to ionizing radiation (IR) or hydrogen peroxide (H2O2). H2O2 treatment was for 10 min at the indicated doses. Error bars indicate s.d. from two and three independent experiments, respectively. The results are normalized to plating efficiencies to focus on the effect of CHD4 depletion upon DNA damage. Note that in the absence of DNA-damaging agent, the viability of CHD4-depleted cells is ∼66% of that of control cells.CC BY-NC-SA · PubMed Central

Figure 6 CHD4 controls the G1/S cell-cycle transition through p53 deacetylation. (A) Fluorescence-activated cell sorting (FACS) profiles of U2OS cells downregulated for CHD4 (siCHD4) compared with control (siLuci). Percentages of cells in G1 are indicated. Nocodazole was used to block cell-cycle progression in mitosis (bottom panels). (B) Western-blot analysis of total extracts from U2OS cells downregulated for CHD4 (siCHD4) compared with control (siLuci) using the indicated antibodies. (C) Quantitative RT–PCR analysis of p21, p53 and β-actin mRNA levels in U2OS cells downregulated for CHD4 (siCHD4) compared with control (siLuci). Error bars indicate s.d. from two independent experiments. (D) Western-blot analysis of p21 induction on total extracts from p53 proficient or deficient HCT116 cells upon CHD4 depletion (C) compared with control siLuciferase (L). + IR: 9 h post-exposure to 10 Gy IR. (E, F) Western-blot analysis of total extracts from U2OS cells treated with the indicated siRNAs. Phleo: 1 h post-exposure to 60 μg/ml Phleomycin. (G) FACS profiles of U2OS cells treated with the indicated siRNAs. Nocodazole was used to block cell-cycle progression in mitosis.CC BY-NC-SA · PubMed Central

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Self-citation
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Jackson, S. P., & Bartek, J. (2009) · Nature · doi:10.1038/nature08467 · Cited by 6,092 · cited 3×
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BackgroundSelf-citation
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“The work must be attributed back to the original author and commercial use is not permitted without specific permission.”
Background
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Vousden, K. H., & Prives, C. (2009) · Cell · doi:10.1016/j.cell.2009.04.037 · Cited by 3,163 · cited 2×
“The work must be attributed back to the original author and commercial use is not permitted without specific permission.”
Background
ATM and ATR Substrate Analysis Reveals Extensive Protein Networks Responsive to DNA Damage
Matsuoka, S., Ballif, B. A., Smogorzewska, A., McDonald, E. R., Hurov, K. E., Luo, J., Bakalarski, C. E., Zhao, Z., Solimini, N., Lerenthal, Y., et al. (2007) · Science · doi:10.1126/science.1140321 · Cited by 3,075 · cited 5×
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BackgroundMethodInfluential
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Background
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Background
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Kruse, J.-P., & Gu, W. (2009) · Cell · doi:10.1016/j.cell.2009.04.050 · Cited by 1,610 · cited 3×
“The work must be attributed back to the original author and commercial use is not permitted without specific permission.”
Background
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Rouleau, M., Patel, A., Hendzel, M. J., Kaufmann, S. H., & Poirier, G. G. (2010) · Nature Reviews Cancer · doi:10.1038/nrc2812 · Cited by 1,298 · cited 1×
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Marques, J. G., Pavlovic, B., Ngo, Q. A., Pedot, G., Roemmele, M., Volken, L., Kisele, S., Perbet, R., Wachtel, M., & Schäfer, B. W. (2023) · Cancer Research · doi:10.1158/0008-5472.can-22-3950 · Cited by 16
The GATAD2B-NuRD complex drives DNA:RNA hybrid-dependent chromatin boundary formation upon DNA damage
Liu, Z., Ajit, K., Wu, Y., Zhu, W., & Gullerová, M. (2024) · The EMBO Journal · doi:10.1038/s44318-024-00111-7 · Cited by 16
“Various speci ﬁ c NuRD subunits are rapidly recruited to loci of DNA damage (Chou et al, 2010; Larsen et al, 2010; Polo et al, 2010; Smeenk et al, 2010).”
Background
Biphasic recruitment of TRF2 to DNA damage sites promotes non-sister chromatid homologous recombination repair
Kong, X., Cruz, G. M. S., Trinh, S., Zhu, X., Berns, M. W., & Yokomori, K. (2018) · Journal of Cell Science · doi:10.1242/jcs.219311 · Cited by 16
“Furthermore, PAR modification at DNA damage sites is critical for the recruitment of chromatin modifying enzymes that promote DNA repair (Ahel et al., 2009; Ayrapetov et al., 2014; Ball and Yokomori, 2011; Chou et al., 2010; Gottschalk et al., 2009; Izhar et al., 2015; Khoury-Haddad et al., 2014; Larsen et al., 2010;…”
Background
Chromatin Remodeling in the Brain-a NuRDevelopmental Odyssey
Larrigan, S., Shah, S. J., Fernandes, J. A. L., & Mattar, P. A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094768 · Cited by 18
“In cell lines, CHD4 has been shown to participate in the DNA damage response [78–80], and CHD4 deficiency has been repeatedly shown to trigger to ATM-dependent intra-S-phase checkpoint activation [31,79,80].”
Background
Laser Microirradiation to Study In Vivo Cellular Responses to Simple and Complex DNA Damage
Kong, X., Cruz, G. M. S., Silva, B. A., Wakida, N. M., Khatibzadeh, N., Berns, M. W., & Yokomori, K. (2018) · Journal of Visualized Experiments · doi:10.3791/56213 · Cited by 17
NEAT1 promotes genome stability via m 6 A methylation-dependent regulation of CHD4Preprint
Mamontova, V., Trifault, B., Gribling-Burrer, A.-S., Bohn, P. S., Boten, L., Preckwinkel, P., Gallant, P., Solvie, D., Ade, C. P., Papadopoulos, D., et al. (2024) · Genes & Development · doi:10.1101/gad.351913.124 · Cited by 16
“The chromodomain helicase DNA binding protein 4 (CHD4) histone deacetylase caught our attention, as it both promotes DSBR and binds several lncRNAs, including NEAT1 (Polo et al. 2010; Hendrickson et al. 2016; Zhao et al. 2018).”
Background
The neuro-glial-vascular interrelations in genomic instability symptoms
Barzilai, A. (2011) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2011.06.001 · Cited by 15
The epigenetic factor CHD4 contributes to metastasis by regulating the EZH2/β-catenin axis and acts as a therapeutic target in ovarian cancer
Wang, J., Zhong, F., Li, J., Yue, H., Li, W., & Lü, X. (2023) · Journal of Translational Medicine · doi:10.1186/s12967-022-03854-1 · Cited by 15
MKP1 phosphatase mediates G1-specific dephosphorylation of H3Serine10P in response to DNA damage
Sharma, A. K., Khan, S. A., Sharda, A., Reddy, D., & Gupta, S. (2015) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2015.06.001 · Cited by 15
Association of the chromodomain helicase DNA‐binding protein 4 (CHD4) missense variation p.D140E with cancer: Potential interaction with smoking
Yamada, M., Sato, N., Ikeda, S., Arai, T., Sawabe, M., Mori, S., Yamada, Y., Muramatsu, M., & Tanaka, M. (2014) · Genes Chromosomes and Cancer · doi:10.1002/gcc.22227 · Cited by 14
“VC 2014 Wiley Periodicals, Inc. GENES, CHROMOSOMES & CANCER 54:122–128 (2015) et al., 2010; Li and Kumar, 2010; Polo et al., 2010; Stanley et al., 2013).”
Background
The Expanding Mi-2/NuRD Complexes: A Schematic Glance
Zhang, Y., & Li, Y. (2010) · Proteomics Insights · doi:10.4137/pri.s6329 · Cited by 15
The Role of the Neuro-Astro-Vascular Unit in the Etiology of Ataxia Telangiectasia
Meshulam, L., Galron, R., Kanner, S., Pittà, M. D., Bonifazi, P., Goldin, M. M., Frenkel, D., Ben‐Jacob, E., & Barzilai, A. (2012) · Frontiers in Pharmacology · doi:10.3389/fphar.2012.00157 · Cited by 14
To Ub or not to Ub: The epic dilemma of histones that regulate gene expression and epigenetic cross-talk
Dasgupta, A., Nandi, S., Gupta, S. D., Roy, S., & Das, C. (2024) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2024.195033 · Cited by 14
Connecting Chromatin Modifying Factors to DNA Damage Response
Lai, W., Li, H., Liu, S., & Tao, Y. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms14022355 · Cited by 13
“Moreover, CHD4 functions as a key regulator of the G1/S cell cycle transition by p53 deacetylation [32].”
Herpesvirus DNA polymerase processivity factors: Not just for DNA synthesis
Cohan, B., & Frappier, L. (2021) · Virus Research · doi:10.1016/j.virusres.2021.198394 · Cited by 13
MTA family of proteins in DNA damage response: mechanistic insights and potential applications
Li, D., Yang, Y., & Kumar, R. (2014) · Cancer and Metastasis Reviews · doi:10.1007/s10555-014-9524-2 · Cited by 13
“Consequently, knockdown of CHD4 sensitizes cells to DNA damage agents and deregulates cell cycle progression [90, 92].”
The Nucleosome Remodeling and Deacetylase Complex in Development and Disease
Basta, J. M., & Rauchman, M. I. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-800802-7.00003-4 · Cited by 14
HJURP is recruited to double-strand break sites and facilitates DNA repair by promoting chromatin reorganization
Serafim, R. B., Cardoso, C. C., Storti, C. B., da Silva, P., Qi, H., Parasuram, R., Navegante, G., Peron, J. P. S., Silva, W. A., Espreáfico, E. M., et al. (2024) · Oncogene · doi:10.1038/s41388-024-02937-1 · Cited by 13
Histone Displacement during Nucleotide Excision Repair
Dinant, C., Bártek, J., & Bekker‐Jensen, S. (2012) · International Journal of Molecular Sciences · doi:10.3390/ijms131013322 · Cited by 13
“chromatin relaxation is CHD4, which has been shown to be recruited to sites of DSBs in a PARP-dependent manner (see also below) [43].”
Background
CHD4 acts as a critical regulator in the survival of spermatogonial stem cells in mice
Li, P., Tang, J., Yu, Z., Jin, C., Wang, Z., Li, M., Zou, D., Mang, X., Liu, J., Lü, Y., et al. (2022) · Biology of Reproduction · doi:10.1093/biolre/ioac162 · Cited by 11
“At the same time, in Chd4MKO mice, the expression of cell cycle-related gene Trp53 was upregulated following Chd4 knockout, which is consistent with the established literature.”
BackgroundInfluential
Streamlined histone-based fluorescence lifetime imaging microscopy (FLIM) for studying chromatin organisation
Sherrard, A., Bishop, P., Panagi, M., Villagomez, M. B., Alibhai, D., & Kaidi, A. (2018) · Biology Open · doi:10.1242/bio.031476 · Cited by 11
“S1B), indicative of their incorporation into chromatin (Polo et al., 2010).”
Self-citation
Dysregulation of cell cycle control caused by overexpression of the oncogene pp32r1 (ANP32C) and the Tyr>His mutant pp32r1Y140H
Buddaseth, S., Göttmann, W., Blasczyk, R., & Huyton, T. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.02.001 · Cited by 11
“Knockdown studies and BrdU incorporation assays demonstrated a specific role of CHD4 in cell cycle progression, in particular as a critical regulator of the G1 to S (G1/S) transition through the control of p53 deacetylation [21,22].”
Background
Remodeler Catalyzed Nucleosome Repositioning: Influence of Structure and Stability
Morgan, A. M., LeGresley, S. E., & Fischer, C. J. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms22010076 · Cited by 11
Gatad2b, associated with the neurodevelopmental syndrome GAND, plays a critical role in neurodevelopment and cortical patterning
Abad, C., Robayo, M. C., Moreno, M. D. M. M., Bernardi, M. T., Otero, M. G., Kosanovic, C., Griswold, A. J., Pierson, T. M., Walz, K., & Young, J. I. (2024) · Translational Psychiatry · doi:10.1038/s41398-023-02678-x · Cited by 9
“NuRD complexes have been implicated in regulating gene transcription, genome stability and DNA repair [11 – 14], as well as controlling events related to cell cycle progression, stem cell differentiation, and cerebral corticogenesis [15, 16].”
Background
VGLL3 modulates chemosensitivity through promoting DNA double-strand break repair
Wu, W. J., Fan, Z., Fu, H., Ma, X., Wang, D., Liu, H., Zhang, C., Zheng, H., Yang, Y., Wu, H., et al. (2024) · Science Advances · doi:10.1126/sciadv.adr2643 · Cited by 9
“HA-CHD4 and pcDNA4TO- GFP-CHD4 were provided by S. Jackson and J. Lukas, respectively ( 51 , 52 ).”
Mutations of ARID1B, PIK3C2B, KMT2B, and FAT1 genes influence clinical outcome in newly diagnosed myeloma
Morawska, M., Kiełbus, M., Paziewska, M., Szelest, M., Karczmarczyk, A., Zaleska, J., Własiuk, P., Giannopoulos, K., & Grząśko, N. (2024) · Cancer Genetics · doi:10.1016/j.cancergen.2024.11.001 · Cited by 11
ATM and ATR checkpoint kinase pathways: A concise review
Chauhan, N., Wagh, V., Joshi, P., & Jariyal, H. (2020) · Advances in Human Biology · doi:10.4103/aihb.aihb_78_19 · Cited by 9
The Chd4 subunit of the NuRD complex regulates Pdx1-controlled genes involved in β-cell function
Davidson, R. K., Weaver, S. A., CASEY, N., Kanojia, S., Hogarth, E., Aguirre, R. S., Sims, E. K., Evans‐Molina, C., & Spaeth, J. M. (2022) · Journal of Molecular Endocrinology · doi:10.1530/jme-22-0011 · Cited by 11
The Tale of CHD4 in DNA Damage Response and Chemotherapeutic Response
Lin, S.-Y., Zhang, J., & Shih, D. J. H. (2019) · Cancer Research and Cellular Therapeutics · doi:10.31579/2640-1053/052 · Cited by 9
“In addition, CHD4 can be phosphorylated by the DNA damage response kinases ATM [34, 35] and ATR [36], and in turn CHD4 can also regulate the Tip60dependent phosphorylation of ATM [37] in response to DNA damage.”
Background
Aberrant chromatin remodeling in gynecological cancer (Review)
Okawa, R., Banno, K., Iida, M., Yanokura, M., Takeda, T., Iijima, M., Irie, H., Nakamura, K., Adachi, M., Umene, K., et al. (2017) · Oncology Letters · doi:10.3892/ol.2017.6891 · Cited by 9
“CHD4 is a catalytic subunit of the NuRD complex that inhibits transcription and repairs DNA damage (52).”
Chromatin Remodulator CHD4: A Potential Target for Cancer Interception
Goswami, K., Venkatachalam, K., Singh, S. P., Rao, C. V., & Madka, V. (2025) · Genes · doi:10.3390/genes16020225 · Cited by 8
“However, the recent study results cannot explain Loss of CHD4 also results in CDC25A degradation and p21 accumulation, leading to cell cycle delay [34,43,45]. the entire complexity of CHD4’s contribution to DNA damage response and cell viability [45,47,48].”
Influential
The crosstalk of m6A-modified RNA with DNA damage repair
Qu, F., & Liu, Y. (2025) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2025.06.012 · Cited by 8
NSUN2 facilitates DICER cleavage of DNA damage-associated R-loops to promote repair
Alagia, A., Ajit, K., Fazio, A. D., Long, Q., & Gullerová, M. (2025) · Nature Communications · doi:10.1038/s41467-025-63220-9 · Cited by 8
The recruitment of ACF1 and SMARCA5 to DNA lesions relies on ADP-ribosylation dependent chromatin unfolding
Jurado, E. P., Smith, R., Bigot, N., Chapuis, C., Timinszky, G., & Huet, S. (2024) · Molecular Biology of the Cell · doi:10.1091/mbc.e23-07-0281 · Cited by 8
“Several chromatin remodelers recruit early to lesions during the DNA damage response (DDR), facilitating efficient double-strand break (DSB) repair via homologous recombination and non homologous end-joining pathways (Lan et al. , 2010; Polo et al. , 2010; Luijsterburg et al. , 2016).”
Background
Frequency and Nature of Genomic Alterations in ERBB2-Altered Urothelial Bladder Cancer
Leary, J. B., Enright, T. J., Bakaloudi, D. R., Basnet, A., Bratslavsky, G., Jacob, J. M., Spiess, P. E., Li, R., Necchi, A., Kamat, A. M., et al. (2024) · Targeted Oncology · doi:10.1007/s11523-024-01056-x · Cited by 9
“Loss of CHD4 leads to accumulation of DNA damage [62]; CDH4 appears to be involved in the repair of both single and double-strand breaks, as well as oxidative damage repair, and exerts cell cycle control at the G1/S transition via regulation of p53 deacetylation [63].”
Monitoring global changes in chromatin compaction states upon localized DNA damage with tools of fluorescence anisotropy
Kesavan, P. S., Bohra, D., Roy, S., & Mazumder, A. (2020) · Molecular Biology of the Cell · doi:10.1091/mbc.e19-08-0417 · Cited by 8
“Molecular Biology of the Cell damage may be relaxed as a response to damage (Park et al., 2006; Polo et al. 2010).”
Background
Germline Genetic Variants and Lung Cancer Survival in African Americans
Jones, C. C., Bush, W. S., Crawford, D. C., Wenzlaff, A. S., Schwartz, A. G., Wiencke, J. K., Wrensch, M., Blot, W. J., Chanock, S. J., Grogan, E. L., et al. (2017) · Cancer Epidemiology Biomarkers & Prevention · doi:10.1158/1055-9965.epi-16-0998 · Cited by 8
“Additionally, CHD4 plays a role in DNA damage response and cell cycle progression (48, 49).”
CHD6 has poly(ADP-ribose)- and DNA-binding domains and regulates PARP1/2-trapping inhibitor sensitivity via abasic site repair
Provencher, L., Nartey, W., Brownlee, P. M., Atkins, A. W., Gagné, J., Baudrier, L., Ting, N. S. Y., Piett, C. G., Fang, S., Pearson, D. D., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-56085-5 · Cited by 8
A LANA peptide inhibits tumor growth by inducing CHD4 protein cleavage and triggers cell death
Miura, H., Wang, K.-H., Inagaki, T., Chuang, F. Y. S., Shimoda, M., Izumiya, C., Watanabe, T., Davis, R. R., Tepper, C. G., Komaki, S., et al. (2024) · Cell chemical biology · doi:10.1016/j.chembiol.2024.10.003 · Cited by 7
The dynamic interplay in chromatin remodeling factors polycomb and trithorax proteins in response to DNA damage
Liu, S., Tao, Y., Chen, X., & Cao, Y. (2011) · Molecular Biology Reports · doi:10.1007/s11033-011-1435-5 · Cited by 7
“novel regulator [54].”
Mitochondrial stress orchestrates chromatin remodeling and longevity via phosphoregulation of the NuRD component LIN-40
Zhou, J., Zhu, D., Wang, Y., Wang, Z., Zhang, N., Huang, X., Zhang, Y., Wang, Y., Wu, X., & Tian, Y. (2025) · Science China Life Sciences · doi:10.1007/s11427-025-2954-3 · Cited by 7
“While phosphoproteomics studies have identified phosphorylation sites on NuRD components, the physiological relevance of these modifications in response to stress or aging remains largely unexplored (Bouazoune and Brehm, 2005; Polo et al., 2010; Sun et al., 2007).”
Genetic Navigation: A Narrative Review of XRCC1 Polymorphism Impact on Platinum-Based Chemotherapy Outcomes in NSCLC Patients
Permatasari, L. I., Afifah, N. N., Ishmatullah, M. H., Intania, R., Halimah, E., & Barliana, M. I. (2025) · Cancer Management and Research · doi:10.2147/cmar.s501420 · Cited by 6
“36 ,37 In addition to aiding recruitment, XRCC1 prevents excessive PARP-1 activity, which can lead to DNA structural entrapment during repair and trigger additional damage.”
CHD4 plays a critical role in arsenite-induced oxidative damage in human urothelial carcinoma
Chang, S., Bin, P.-J., Luo, C., & Chai, C. (2022) · Pathology - Research and Practice · doi:10.1016/j.prp.2022.154173 · Cited by 6
NuRD Alert! NuRD Regulates the DNA Damage Response
Smeenk, G., & van Attikum, H. (2011) · Epigenomics · doi:10.2217/epi.10.79 · Cited by 6
Chromatin Remodelers and Their Way of Action
Manelytė, L., & Längst, G. (2013) · InTech eBooks · doi:10.5772/55683 · Cited by 6
“Several studies demonstrated the targeting of Chd4 to sites of DNA double strand breaks in a PARP dependent manner [87].”
Background
Chromodomain helicase DNA binding protein 4 in cell fate decisions
Laureano, A., Kim, J.-H., Martinez, E. A., & Kwan, K. Y. (2023) · Hearing Research · doi:10.1016/j.heares.2023.108813 · Cited by 5
Zinc finger transcription factor CASZ1b is involved in the DNA damage response in live cells
Liu, Z., Kruhlak, M. J., & Thiele, C. J. (2023) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2023.04.085 · Cited by 4
γH2AX prefers late replicating metaphase chromosome regions
Reyes-Ábalos, A. L., Liddle, P., Folle, G. A., & Tomaso, M. V. D. (2018) · Mutation Research/Genetic Toxicology and Environmental Mutagenesis · doi:10.1016/j.mrgentox.2018.06.001 · Cited by 6
The PARP1/ARTD1-Mediated Poly-ADP-Ribosylation and DNA Damage Repair in B Cell Diversification
Lasola, J. J., Hodgson, A., Sun, X., & Wan, F. (2014) · Antibodies · doi:10.3390/antib3010037 · Cited by 4
“Conversely, recent findings outlined a role for PARP1/ARTD1 in transcriptional silencing by triggering chromatin compaction, which can be best exemplified by the finding that several components of the NuRD complex, including chromodomain helicase DNA binding protein 4 (CHD4) are recruited by PARP1/ARTD1 and execute hi…”
Genetically altered cancer epigenome
Tang, M., Luo, H., & Lu, J. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-799958-6.00012-3 · Cited by 4
Cell Cycle and DNA Damage Response in Postmitotic Neurons
Kruman, I. I. (2011) · InTech eBooks · doi:10.5772/20859 · Cited by 3
“It is involved in buildup of the chromatin remodeling factors ALC1 and CHD4 (Ahel et al., 2009; Chou et al., 2010; Gottschalk et al., 2009; Polo et al., 2010), the Polycomb histone-modifying complex (Chou et al., 2010), and the histone variant macro H2A (Timinszky et al., 2009).”
Background
Oncogenic acidic nuclear phosphoproteins ANP32C/D are novel clients of heat shock protein 90
Yuzefovych, Y., Blasczyk, R., & Huyton, T. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2015.06.007 · Cited by 3
Mouse CHD4-NURD is required for neonatal spermatogonia survival and normal gonad developmentPreprint
de Castro, R. O., Previato, L., Carbajal, A., Goitea, V. E., Griffin, C. T., & Pezza, R. J. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/687137 · Cited by 3
“Given its positive impact on survival following irradiation, current models predict that CHD4 promotes a permissive chromatin environment for proper DSB repair [9, 11, 29], a model that well could explain the phenotype we observed.”
BackgroundInfluential
The chromatin remodeller CHD4 regulates transcription factor binding to both prevent activation of silent enhancers and maintain active regulatory elementsPreprint
Koulle, A., Ogundele, O., Shah, D., Baker, I. M., Lopez, M., Lando, D., Reynolds, N., Ragheb, R., Laue, E. D., & Hendrich, B. (2025) · eLife · doi:10.7554/elife.109280 · Cited by 6
The nephronophthisis protein GLIS2 / NPHP7 is required for the DNA damage response in kidney tubular epithelial cells
Ebert, L. K., Schloesser, L., Frech, L. E., Jain, M., Dafinger, C., Liebau, M. C., Benzing, T. R., Schermer, B., & Slaats, G. G. G. (2025) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00076.2025 · Cited by 2
CD276 immature glycosylation drives colorectal cancer aggressiveness and T cell mediated immune escape
Soares, J., Ferreira, D., Miranda, A., Gonçalves, M., Relvas‐Santos, M., Brandão, A., Paulo, P., Cotton, S., Freitas, R., Magalhães, M., et al. (2026) · Cell Communication and Signaling · doi:10.1186/s12964-026-02672-y · Cited by 4
Chromatin remodeling protein CHD4 regulates axon guidance of spiral ganglion neurons in the developing cochleaPreprint
Kim, J., Martinez, E. A., Qiu, J., Laureano, A., Hinman, A. M., Ni, J. Z., & Kwan, K. Y. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.01.31.578202 · Cited by 2
CHD4 acts as a prognostic factor and drives radioresistance in HPV negative HNSCC
Geyer, F., Geyer, M., Reuning, U., Klapproth, S., Wolff, K., & Nieberler, M. (2024) · Scientific Reports · doi:10.1038/s41598-024-58958-z · Cited by 1
“Together with NuRD, CHD4 controls p53 deacetylation, hence being an important regulator of the G 1 /S transition 44,45 .”
Background
miR-194-3 Regulates Proliferation and Apoptosis of Follicular Granulosa Cells by Targeting CHD4 in Zhedong White Geese
Zheng, P., Zang, Z., Wang, S., Zeng, C., Pan, Y., Zhang, Y., Yue, S., Liu, S., Huang, H., & Zhao, X. (2025) · Animals · doi:10.3390/ani15182676 · Cited by 1
“A core ATPase subunit of the NuRD (nucleosome remodeling and deacetylase) chromatin remodeling complex is known to play a crucial role in DNA damage repair and cell cycle regulation [27].”

Authors: Polo, S. E., Kaidi, A., Baskcomb, L., Galanty, Y., & Jackson, S. P.
Affiliations: University of Cambridge (GB)
Corresponding author: Jackson, Stephen P
ORCID: Polo, Sophie E
Kaidi, Abderrahmane
Galanty, Yaron
Jackson, Stephen P
Venue: The EMBO Journal
Publisher: Springer Science and Business Media LLC
Published: 2010-08-06
Volume: 29
Issue: 18
Pages: 3130-3139
ISSN: 0261-4189 (ISSN-L)
1460-2075
DOI: 10.1038/emboj.2010.188
PMC: PMC2944064
OpenAlex: W2020084014
Cited by: 374
References: 56
Citations by year: 2026: 13 · 2025: 14 · 2024: 20 · 2023: 17 · 2022: 26 · 2021: 17 · 2020: 22 · 2019: 18 · 2018: 18 · 2017: 35 · 2016: 24 · 2015: 17 · 2014: 31 · 2013: 34 · 2012: 31
FWCI: 13.30
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by-nc-sa
creativecommons.org/licenses/by-nc-sa/3.0/ (tdm)
creativecommons.org/licenses/by-nc-sa/3.0/ (vor)
Locations: The EMBO Journal (publishedVersion, cc-by-nc-sa)
PubMed Central (publishedVersion, cc-by-nc-sa)
PubMed (publishedVersion)
Explore Bristol Research (submittedVersion)
Funders: Wellcome Trust
Cancer Research UK (11224, A5290, A4361)
European Commission (512113, 201630, LSHG-CT-2005-512113)
Directorate for Biological Sciences
Biotechnology and Biological Sciences Research Council
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chromatin Remodeling and Cancer
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
Keywords: CHD4, chromatin remodeling, NuRD complex, DNA damage response, cell cycle regulation, G1/S transition, p53 deacetylation, ATM phosphorylation, DNA double-strand break repair, poly(ADP-ribose), poly(ADP-ribose) polymerase, genome stability, transcriptional repressor
MeSH terms: Animals, Autoantigens, Cell Cycle, DNA Damage, DNA Helicases, DNA-Binding Proteins, Fluorescent Antibody Technique, Histones, Humans, Phosphorylation, Poly Adenosine Diphosphate Ribose, RNA, Messenger, Blotting, Western, Tumor Suppressor Protein p53, Protein Serine-Threonine Kinases, Mice, Knockout, Cell Cycle Proteins, Reverse Transcriptase Polymerase Chain Reaction, Tumor Suppressor Proteins, Chromatin Assembly and Disassembly, Immunoprecipitation, Mice, Mi-2 Nucleosome Remodeling and Deacetylase Complex, Ataxia Telangiectasia Mutated Proteins

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Regulation of DNA‐damage responses and cell‐cycle progression by the chromatin remodelling factor CHD4

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