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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A Systematic Analysis of Factors Localized to Damaged Chromatin Reveals PARP-Dependent Recruitment of Transcription Factors
Izhar, L., Adamson, B., Ciccia, A., Lewis, J., Vaites, L. P., Leng, Y., Liang, A. C. T., Westbrook, T. F., Harper, J. W., & Elledge, S. J. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.04.053 · Cited by 178
“…(PAR) structures and are responsible for the recruitment of a number of factors to sites of DNA damage, including ALC1, RBMX, and components of MRN and NuRD complexes, among others (Adamson et al., 2012; Ahel et al., 2009; Chou et al., 2010; Haince et al., 2008; Polo et al., 2010).”
Influential
Plant Homeodomain (PHD) Fingers of CHD4 Are Histone H3-binding Modules with Preference for Unmodified H3K4 and Methylated H3K9
Mansfield, R. E., Musselman, C. A., Kwan, A. H., Oliver, S. S., Garske, A. L., Davrazou, F., Denu, J. M., Kutateladze, T. G., & Mackay, J. P. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.208207 · Cited by 177
Reprogramming cellular events by poly(ADP-ribose)-binding proteins
Krietsch, J., Rouleau, M., Pic, É., Ethier, C., Dawson, T. M., Dawson, V. L., Masson, J., Poirier, G. G., & Gagné, J. (2012) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2012.12.005 · Cited by 185
PARP1-Driven Poly-ADP-Ribosylation Regulates BRCA1 Function in Homologous Recombination–Mediated DNA Repair
Hu, Y., Petit, S. A., Ficarro, S. B., Toomire, K. J., Xie, A., Lim, E., Cao, S. A., Park, E., Eck, M. J., Scully, R., et al. (2014) · Cancer Discovery · doi:10.1158/2159-8290.cd-13-0891 · Cited by 181
“Among their interacting partners are proteins recently shown to be involved in cellular responses to DSBs, including SFPQ (15), CHD4 (16), and UBR5 (17) (Supplementary Fig.”
PARP activation regulates the RNA-binding protein NONO in the DNA damage response to DNA double-strand breaks
Krietsch, J., Caron, M., Gagné, J., Ethier, C., Vignard, J., Vincent, M., Rouleau, M., Hendzel, M. J., Poirier, G. G., & Masson, J. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks798 · Cited by 166
“To date, many proteins have been shown to be recruited in a PAR-dependent manner by cell imaging techniques: MRE11 (6), NBS1 (6), APLF (46), XRCC1 (57), CHD4 (58), NuRD (59) and ALC1 (47).”
Background
Quantitative proteomics profiling of the poly(ADP-ribose)-related response to genotoxic stress
Gagné, J., Pic, É., Isabelle, M., Krietsch, J., Éthier, C., Paquet, É. R., Kelly, I., Boutin, M., Moon, K., Foster, L. J., et al. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks486 · Cited by 165
“The recent identification of chromatinassociated proteins whose recruitment to DNA damage sites is pADPr-dependent [e.g.: CHD4 (38,73), MTA1(73), MRE11(74), NBS1(74), ALC1(39,40), APLF (75,76), XRCC1 (68), BMI-1 (77), MEL-18 (73)] also points towards this model.”
Epigenetic regulation of autophagy by the methyltransferase EZH2 through an MTOR-dependent pathway
Wei, F.-Z., Cao, Z., Wang, X., Wang, H., Cai, M.-Y., Li, T., Hattori, N., Wang, D., Du, Y., Song, B., et al. (2015) · Autophagy · doi:10.1080/15548627.2015.1117734 · Cited by 161
DDB2 promotes chromatin decondensation at UV-induced DNA damage
Luijsterburg, M. S., Lindh, M., Ács, K., Vrouwe, M. G., Pines, A., van Attikum, H., Mullenders, L. H. F., & Dantuma, N. P. (2012) · The Journal of Cell Biology · doi:10.1083/jcb.201106074 · Cited by 176
“Additionally, the DNA damage– induced reduction in histone density also required the activity of PARP1, which has recently been linked to chromatin remodeling in response to double-strand DNA breaks (Ahel et al., 2009; Gottschalk et al., 2009; Chou et al., 2010; Polo et al., 2010).”
PARP1-dependent recruitment of KDM4D histone demethylase to DNA damage sites promotes double-strand break repair
Khoury-Haddad, H., Guttmann‐Raviv, N., Ipenberg, I., Huggins, D. J., Jeyasekharan, A. D. D., & Ayoub, N. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1317585111 · Cited by 148
“Similarly, it was recently shown that PARP1 and Really Interesting New Gene finger protein (RNF)8 ubiquitin ligase regulate the recruitment of the catalytic subunit of the NuRD repressor complex, CHD4, to DNA-breakage sites (49, 61).”
BackgroundResultInfluential
Histone demethylase KDM5B is a key regulator of genome stability
Li, X., Liu, L., Yang, S., Song, N., Zhou, X., Gao, J., Yu, N., Shan, L., Wang, Q., Liang, J., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1324036111 · Cited by 148
Poly(ADP-ribosyl)ation links the chromatin remodeler SMARCA5/SNF2H to RNF168-dependent DNA damage signaling
Smeenk, G., Wiegant, W. W., Marteijn, J. A. F., Luijsterburg, M. S., Sroczynski, N., Costelloe, T., Romeijn, R. J., Pastink, A., Mailand, N., Vermeulen, W., et al. (2012) · Journal of Cell Science · doi:10.1242/jcs.109413 · Cited by 154
“itself and acceptor proteins, directs the recruitment of the chromatin remodeling enzymes ALC1 and CHD4 to DSBs (Ahel et al., 2009; Chou et al., 2010; Gottschalk et al., 2009; Luijsterburg et al., 2012a; Polo et al., 2010).”
Background
Chromatin and the DNA damage response: The cancer connection
Luijsterburg, M. S., & van Attikum, H. (2011) · Molecular Oncology · doi:10.1016/j.molonc.2011.06.001 · Cited by 148
Snf2-family proteins: chromatin remodellers for any occasion
Ryan, D., & Owen‐Hughes, T. (2011) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2011.07.022 · Cited by 148
“Kinetic analysis of Alc1 retention at laserinduced damage sites suggest Alc1 acts at an early stage in the DDR. 48.”
BackgroundInfluential
De Novo Mutations in CHD4 , an ATP-Dependent Chromatin Remodeler Gene, Cause an Intellectual Disability Syndrome with Distinctive Dysmorphisms
Weiss, K., Terhal, P. A., Cohen, L., Bruccoleri, M., Irving, M. D., Martinez, A. F., Rosenfeld, J. A., Machol, K., Yang, Y., Liu, P., et al. (2016) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2016.08.001 · Cited by 139
HDAC Inhibitors
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Automodification switches PARP-1 function from chromatin architectural protein to histone chaperone
Muthurajan, U. M., Chassé, M. H., Hieb, A. R., Clark, N., Kramer, M., Yao, T., & Luger, K. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1405005111 · Cited by 139
The multifaceted influence of histone deacetylases on DNA damage signalling and DNA repair
Roos, W. P., & Krumm, A. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw922 · Cited by 142
“For DSBs, PARP1 and the PAR chains cause the recruitment of the nucleosome remodelling deacetylase (NuRD) complex (100,101) and the polycomb group (PcG) proteins (101–103), all of which are essential for the effective repair of DSBs (100,102–104) (Figure 1C).”
Background
The histone demethylase LSD1/KDM1A promotes the DNA damage response
Mosammaparast, N., Kim, H., Laurent, B., Zhao, Y. J., Lim, H. J., Majid, M. C., Dango, S., Luo, Y., Hempel, K., Sowa, M. E., et al. (2013) · The Journal of Cell Biology · doi:10.1083/jcb.201302092 · Cited by 140
“…chromatin marks, such as methylation of H3K9, and recruitment of the NuRD–CHD4 complex are two other examples of a transient, repressive chromatin state that appear to be critical for the DDR (Chou et al., 2010; Larsen et al., 2010; Polo et al., 2010; Smeenk et al., 2010; Chiolo et al., 2011).”
Influential
Acetylation Reader Proteins: Linking Acetylation Signaling to Genome Maintenance and Cancer
Gong, F., Chiu, L.-Y., & Miller, K. M. (2016) · PLoS Genetics · doi:10.1371/journal.pgen.1006272 · Cited by 137
NuRD–ZNF827 recruitment to telomeres creates a molecular scaffold for homologous recombination
Conomos, D., Reddel, R. R., & Pickett, H. A. (2014) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2877 · Cited by 129
The NuRD complex cooperates with DNMTs to maintain silencing of key colorectal tumor suppressor genes
Cai, Y., Geutjes, E.-J., de Lint, K., Roepman, P., Bruurs, L. J. M., Yu, L., Wang, W., van Blijswijk, J., Mohammad, H. P., de Rink, I., et al. (2013) · Oncogene · doi:10.1038/onc.2013.178 · Cited by 135
The Chromatin Response to DNA Breaks: Leaving a Mark on Genome Integrity
Smeenk, G., & van Attikum, H. (2013) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061809-174504 · Cited by 135
“In contrast, both RNF8 and PARP activity appeared to contribute to CHD4 assembly at sites of DNA damage (132, 135).”
Background
The poly(ADP-ribose)-dependent chromatin remodeler Alc1 induces local chromatin relaxation upon DNA damage
Sellou, H., Lebeaupin, T., Chapuis, C., Smith, R., Hegele, A., Singh, H. R., Kozłowski, M., Bultmann, S., Ladurner, A. G., Timinszky, G., et al. (2016) · Molecular Biology of the Cell · doi:10.1091/mbc.e16-05-0269 · Cited by 138
“Additionally, PARylation is also involved in the recruitment and the regulation of several chromatin-remodeling enzymes whose ATP-dependent activity could promote chromatin relaxation (Chou et al., 2010; Polo et al., 2010; Smeenk et al., 2013).”
Background
The recognition and removal of cellular poly( ADP ‐ribose) signals
Barkauskaite, E., Jankevicius, G., Ladurner, A. G., Ahel, I., & Timinszky, G. (2013) · FEBS Journal · doi:10.1111/febs.12358 · Cited by 130
lncRNA PAPAS tethered to the rDNA enhancer recruits hypophosphorylated CHD4/NuRD to repress rRNA synthesis at elevated temperaturesPreprint
Zhao, Z., Cetin, N. S., Song, C., & Grummt, I. (2018) · Genes & Development · doi:10.1101/gad.311688.118 · Cited by 120
“CHD4 is phosphorylated at multiple sites (Bouazoune and Brehm 2005; Polo et al. 2010; Urquhart et al. 2011).”
Structure and Mechanisms of Lysine Methylation Recognition by the Chromodomain in Gene Transcription
Yap, K. L., & Zhou, M. (2011) · Biochemistry · doi:10.1021/bi101885m · Cited by 126
“CHD4 (Mi-2b) Refs (46,108-111) NuRD complex; checkpoint signaling and DNA damage repair; promotes CD4 gene expression during T cell development.”
Background
CREBBP and p300 lysine acetyl transferases in the DNA damage response
Dutto, I., Scalera, C., & Prosperi, E. (2017) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-017-2717-4 · Cited by 118
“In fact, for other important DDR players, the information available indicates that p300/CBP may interact with them, while there is no evidence of their acetylation.”
BackgroundInfluential
CHD3 and CHD4 form distinct NuRD complexes with different yet overlapping functionality
Hoffmeister, H., Fuchs, A., Erdel, F., Pinz, S., Gröbner-Ferreira, R., Bruckmann, A., Deutzmann, R., Schwartz, U., Maldonado, R., Huber, C., et al. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx711 · Cited by 118
Chromodomain Helicase DNA-binding Protein 4 (CHD4) Regulates Homologous Recombination DNA Repair, and Its Deficiency Sensitizes Cells to Poly(ADP-ribose) Polymerase (PARP) Inhibitor Treatment
Pan, M., Hsieh, H.-J., Dai, H., Hung, W.-C., Li, K., Peng, G., & Lin, S. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.287037 · Cited by 118
Chromatin regulation: How complex does it get?
Meier, K., & Brehm, A. (2014) · Epigenetics · doi:10.4161/15592294.2014.971580 · Cited by 114
A new non‐catalytic role for ubiquitin ligase RNF8 in unfolding higher‐order chromatin structure
Luijsterburg, M. S., Ács, K., Ackermann, L., Wiegant, W. W., Bekker‐Jensen, S., Larsen, D. H., Khanna, K. K., van Attikum, H., Mailand, N., & Dantuma, N. P. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.104 · Cited by 117
“Endogenous CHD4 was recruited to laser-generated DSBs marked by phosphorylated histone H2AX ( g H2AX; Figure 6A), in line with several recent reports (Chou et al , 2010; Larsen et al , 2010; Polo et al , 2010; Smeenk et al , 2010).”
Influential
Patching Broken DNA: Nucleosome Dynamics and the Repair of DNA Breaks
Gürsoy-Yüzügüllü, Ö., House, N. C. M., & Price, B. D. (2015) · Journal of Molecular Biology · doi:10.1016/j.jmb.2015.11.021 · Cited by 118
The tale of a tail: histone H4 acetylation and the repair of DNA breaks
Dhar, S., Gürsoy-Yüzügüllü, Ö., Parasuram, R., & Price, B. D. (2017) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2016.0284 · Cited by 123
A team of heterochromatin factors collaborates with small RNA pathways to combat repetitive elements and germline stress
McMurchy, A. N., Stempor, P., Gaarenstroom, T., Wysolmerski, B., Yan, D., Ausiannikava, D., Appert, A., Huang, N., Kolasinska-Zwierz, P., Sapetschnig, A., et al. (2017) · eLife · doi:10.7554/elife.21666 · Cited by 106
PARP3 affects the relative contribution of homologous recombination and nonhomologous end-joining pathways
Beck, C., Boehler, C., Guirouilh‐Barbat, J., Bonnet, M.-E., Illuzzi, G., Rondé, P., Gauthier, L., Magroun, N., Rajendran, A., López, B. S., et al. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku174 · Cited by 126
“The alternative pathway (A-EJ) is initiated by an Mre11-mediated end-resection activity in a manner similar to HR and involves additional proteins such as PARP1, XRCC1, DNA ligase III and histone H1 (14–20).”
BackgroundInfluential
ZMYND8 Co-localizes with NuRD on Target Genes and Regulates Poly(ADP-Ribose)-Dependent Recruitment of GATAD2A/NuRD to Sites of DNA Damage
Spruijt, C. G., Luijsterburg, M. S., Menafra, R., Lindeboom, R. G. H., Jansen, P. W. T. C., Edupuganti, R. R., Baltissen, M. P. A., Wiegant, W. W., Voelker-Albert, M., Matarese, F., et al. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.09.037 · Cited by 114
“This could reconcile our results with previous studies and possibly explain how both PAR and ZMYND8 could stimulate the recruitment of CHD4 and MBD2 (Chou et al., 2010; Luijsterburg et al., 2012; Polo et al., 2010; Sun et al., 2016).”
BackgroundResultInfluential
Regulation of DNA Repair Mechanisms: How the Chromatin Environment Regulates the DNA Damage Response
Stadler, J., & Richly, H. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18081715 · Cited by 110
“The chromatin surrounding DSBs is rapidly and transiently PARylated (Figure 2) causing the recruitment of the NuRD complex [72,73], which harbors both ATP-dependent chromatin remodeling and histone deacetylase activities.”
Background
Metastasis-Associated Protein 1/Nucleosome Remodeling and Histone Deacetylase Complex in Cancer
Li, D., Pakala, S. B., Nair, S. S., Eswaran, J., & Kumar, R. (2012) · Cancer Research · doi:10.1158/0008-5472.can-11-2345 · Cited by 108
CHD chromatin remodelers and the transcription cycle
Murawska, M., & Brehm, A. (2011) · Transcription · doi:10.4161/trns.2.6.17840 · Cited by 108
PHF6 Interacts with the Nucleosome Remodeling and Deacetylation (NuRD) Complex
Todd, M. A. M., & Picketts, D. J. (2012) · Journal of Proteome Research · doi:10.1021/pr3004369 · Cited by 107
SIRT6 coordinates with CHD4 to promote chromatin relaxation and DNA repair
Hou, T., Cao, Z., Zhang, J., Tang, M., Tian, Y., Li, Y., Lu, X., Chen, Y., Wang, H., Wei, F., et al. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa006 · Cited by 96
“We thus proposed that SIRT6 and CHD4 may coordinate their action in DDR.”
BackgroundInfluential
The Cardiac TBX5 Interactome Reveals a Chromatin Remodeling Network Essential for Cardiac Septation
Wasson, L. K., Steimle, J. D., Greco, T. M., Gomez, N. C., Dorr, K. M., Kweon, J., Temple, B. R. S., Yang, X. H., Wilczewski, C. M., Davis, I. J., et al. (2016) · Developmental Cell · doi:10.1016/j.devcel.2016.01.009 · Cited by 96
“GFP tagged full length, C-terminal, and N-terminal human CHD4 constructs were generously provided by Stephen Jackson (Cambridge) (Polo et al., 2010).”
Background
CHD4 in the DNA-damage response and cell cycle progression: not so NuRDy now
O’Shaughnessy, A., & Hendrich, B. (2013) · Biochemical Society Transactions · doi:10.1042/bst20130027 · Cited by 97
The role of poly(ADP-ribosyl)ation in DNA damage response and cancer chemotherapy
Li, M., & Yu, X. (2014) · Oncogene · doi:10.1038/onc.2014.295 · Cited by 99
Defeating EpCAM+ liver cancer stem cells by targeting chromatin remodeling enzyme CHD4 in human hepatocellular carcinoma
Nio, K., Yamashita, T., Okada, H., Kondo, M., Hayashi, T., Hara, Y., Nomura, Y., Zeng, S. S., Yoshida, M., Hayashi, T., et al. (2015) · Journal of Hepatology · doi:10.1016/j.jhep.2015.06.009 · Cited by 98
“Recent studies have shown the importance of CHD4 in response to ionizing radiation and PARP inhibitors [29-32, 38].”
Background
Nucleosome-CHD4 chromatin remodeler structure maps human disease mutations
Farnung, L., Ochmann, M., & Cramer, P. (2020) · eLife · doi:10.7554/elife.56178 · Cited by 95
“It is essential for cell cycle progression (Polo et al., 2010), DNA damage response (Larsen et al.”
Background
Poly(ADP-ribosyl)ation in regulation of chromatin structure and the DNA damage response
Tallis, M., Morra, R., Barkauskaite, E., & Ahel, I. (2013) · Chromosoma · doi:10.1007/s00412-013-0442-9 · Cited by 100
“PARP1 is involved in the early recruitment of theMRN complex to DSBs (Haince et al. 2008) and interacts with cNHEJ components such as WRN (Adelfalk et al. 2003), Ku (Li et al. 2004) and DNAPK (Spagnolo et al. 2012).”
BackgroundInfluential
Initiation of DNA double strand break repair: signaling and single-stranded resection dictate the choice between homologous recombination, non-homologous end-joining and alternative end-joining.
Grabarz, A., Barascu, A., Guirouilh‐Barbat, J., & López, B. S. (2012) · Europe PMC (PubMed Central) · Cited by 93
Preserving genome integrity and function: the DNA damage response and histone modifications
Kim, J. J., Lee, S. Y., & Miller, K. M. (2019) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2019.1620676 · Cited by 96
“PARP also promotes the recruitment of the ZMYND8-NuRD chromatin remodeling complex to damaged chromatin where it participates in repressing transcription in the vicinity of DSBs (Chou et al. 2010; Polo et al. 2010; Gong et al. 2015; Spruijt et al. 2016).”
Background
Nucleosome remodelers in double-strand break repair
Seeber, A., Hauer, M., & Gasser, S. M. (2013) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2012.12.008 · Cited by 92
CHD3 and CHD4 recruitment and chromatin remodeling activity at DNA breaks is promoted by early poly(ADP-ribose)-dependent chromatin relaxation
Smith, R., Sellou, H., Chapuis, C., Huet, S., & Timinszky, G. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky334 · Cited by 100
Mi-2/NuRD complex function is required for normal S phase progression and assembly of pericentric heterochromatin
Sims, J. K., & Wade, P. A. (2011) · Molecular Biology of the Cell · doi:10.1091/mbc.e11-03-0258 · Cited by 87
“3100 | J. K. Sims and P. A. Wade Molecular Biology of the Cell mal chromatin architecture, including the Mi-2/NuRD complex (Sillibourne et al., 2007; Pegoraro et al., 2009; Chou et al., 2010; Cohet et al., 2010; Larsen et al., 2010; Misteli, 2010; Polo et al., 2010; Smeenk et al., 2010).”
Influential
NELF‐E is recruited to DNA double‐strand break sites to promote transcriptional repression and repair
Awwad, S. W., Abu‐Zhayia, E. R., Guttmann‐Raviv, N., & Ayoub, N. (2017) · EMBO Reports · doi:10.15252/embr.201643191 · Cited by 95
A Poly-ADP-Ribose Trigger Releases the Auto-Inhibition of a Chromatin Remodeling Oncogene
Singh, H. R., Nardozza, A. P., Möller, I. R., Knobloch, G., Kistemaker, H. A. V., Hassler, M., Harrer, N., Blessing, C., Eustermann, S., Kotthoff, C., et al. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.11.019 · Cited by 88
“Sites of high PARP1 activity in vivo recruit ATP-dependent remodelers, including ALC1 (Amplified in Liver Cancer 1; also known as CHD1L), CHD2, CHD4, SMARCA5/SNF2H and Drosophila Mi-2 (Chou et al., 2010; Murawska et al., 2011; Polo et al., 2010; Smeenk et al., 2013).”
Background
Histone H3 Lysine 14 (H3K14) Acetylation Facilitates DNA Repair in a Positioned Nucleosome by Stabilizing the Binding of the Chromatin Remodeler RSC (Remodels Structure of Chromatin)
Duan, M., & Smerdon, M. J. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.540732 · Cited by 84
CTCF facilitates DNA double-strand break repair by enhancing homologous recombination repair
Hilmi, K., Jangal, M., Marques, M., Zhao, T., Saad, A., Zhang, C., Luo, V. M., Syme, A., Rejon, C. A., Yu, Z., et al. (2017) · Science Advances · doi:10.1126/sciadv.1601898 · Cited by 81
SALL1 functions as a tumor suppressor in breast cancer by regulating cancer cell senescence and metastasis through the NuRD complex
Ma, C., Wang, F., Han, B., Zhong, X., Si, F., Ye, J., Hsueh, E. C., Robbins, L., Kiefer, S. M., Zhang, Y., et al. (2018) · Molecular Cancer · doi:10.1186/s12943-018-0824-y · Cited by 79
“of the G1/S cell cycle transition and ATM-associated DNA damage responses [56].”
Background
Neutralizing Gatad2a-Chd4-Mbd3/NuRD Complex Facilitates Deterministic Induction of Naive Pluripotency
Mor, N., Rais, Y., Sheban, D., Peles, S., Aguilera-Castrejon, A., Zviran, A., Elinger, D., Viukov, S., Geula, S., Krupalnik, V., et al. (2018) · Cell Stem Cell · doi:10.1016/j.stem.2018.07.004 · Cited by 79
Crosstalk between ubiquitin and other post-translational modifications on chromatin during double-strand break repair
Zhao, Y. J., Brickner, J. R., Majid, M. C., & Mosammaparast, N. (2014) · Trends in Cell Biology · doi:10.1016/j.tcb.2014.01.005 · Cited by 79
“Originally identified as a key component of a histone deacetylase complex that promotes transcriptional repression [58], CHD4/NuRD binds directly to poly-ADP-ribose and requires PARP activity for its recruitment to damage sites [55, 56].”

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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