Ring finger protein RNF169 antagonizes the ubiquitin-dependent signaling cascade at sites of DNA damage.
Open accessAbstract
Ubiquitin signals emanating from DNA double-strand breaks (DSBs) trigger the ordered assembly of DNA damage mediator and repair proteins. This highly orchestrated process is accomplished, in part, through the concerted action of the RNF8 and RNF168 E3 ligases, which have emerged as core signaling intermediates that promote DSB-associated ubiquitylation events. In this study, we report the identification of RNF169 as a negative regulator of the DNA damage signaling cascade. We found that RNF169 interacted with ubiquitin structures and relocalized to DSBs in an RNF8/RNF168-dependent manner. Moreover, ectopic expression of RNF169 attenuated ubiquitin signaling and compromised 53BP1 accumulation at DNA damage sites, suggesting that RNF169 antagonizes RNF168 functions at DSBs. Our study unveils RNF169 as a component in DNA damage signal transduction and adds to the complexity of regulatory ubiquitylation in genome stability maintenance.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
RNF168 promotes 53BP1 and BRCA1 localization to DSBs, while RNF169 competes with 53BP1 and BRCA1 for ubiquitin binding and inhibits this binding.
“While RNF168 promotes 53BP1 and BCRA1 localization to sites of DSBs, RNF169 is a direct inhibitor of this binding. This is because, once RNF168 synthesizes H2A/H2AX ubiquitin chains, RNF169 competes with 53BP1 and BRCA1 for ubiquitin binding (Chen et al., 2012; Panier et al., 2012; Poulsen et al., 2012).”
From USP7 Is a Master Regulator of Genome Stability (2020) · cites this paper as Chen et al., 2012
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
RNF8 Ubiquitylates Histones at DNA Double-Strand Breaks and Promotes Assembly of Repair Proteins
Mailand, N., Bekker‐Jensen, S., Kildegaard, H. F., Melander, F., Bártek, J., Lukas, C., & Lukas, J. (2007) · Cell · doi:10.1016/j.cell.2007.09.040 · Cited by 1,153 · see citing works
Dynamics of DNA damage response proteins at DNA breaks: a focus on protein modifications
Polo, S. E., & Jackson, S. P. (2011) · Genes & Development · doi:10.1101/gad.2021311 · Cited by 1,092 · see citing works
RNF8 Transduces the DNA-Damage Signal via Histone Ubiquitylation and Checkpoint Protein Assembly
Huen, M. S. Y., Grant, R. A., Manke, I. A., Minn, K. T., Yu, X., Yaffe, M. B., & Chen, J. (2007) · Cell · doi:10.1016/j.cell.2007.09.041 · Cited by 1,027 · see citing works
Self-citationDoil, C., Mailand, N., Bekker‐Jensen, S., Ménard, P., Larsen, D. H., Pepperkok, R., Ellenberg, J., Panier, S., Durocher, D., Bártek, J., et al. (2009) · Cell · doi:10.1016/j.cell.2008.12.041 · Cited by 938 · see citing works
Orchestration of the DNA-Damage Response by the RNF8 Ubiquitin Ligase
Kolas, N. K., Chapman, J. R., Nakada, S., Ylanko, J., Chahwan, R., Sweeney, F. D., Panier, S., Mendez, M., Wildenhain, J., Thomson, T. M., et al. (2007) · Science · doi:10.1126/science.1150034 · Cited by 900 · see citing works
The RIDDLE Syndrome Protein Mediates a Ubiquitin-Dependent Signaling Cascade at Sites of DNA Damage
Stewart, G. S., Panier, S., Townsend, K., Al-Hakim, A., Kolas, N. K., Miller, E. S., Nakada, S., Ylanko, J., Olivarius, S., Mendez, M., et al. (2009) · Cell · doi:10.1016/j.cell.2008.12.042 · Cited by 757 · see citing works
ATM-Dependent Chromatin Changes Silence Transcription In cis to DNA Double-Strand Breaks
Shanbhag, N. M., Rafalska-Metcalf, I. U., Balane-Bolivar, C., Janicki, S. M., & Greenberg, R. A. (2010) · Cell · doi:10.1016/j.cell.2010.04.038 · Cited by 737 · see citing works
Crosstalk between histone modifications during the DNA damage response
van Attikum, H., & Gasser, S. M. (2009) · Trends in Cell Biology · doi:10.1016/j.tcb.2009.03.001 · Cited by 515 · see citing works
Wang, B., & Elledge, S. J. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0710061104 · Cited by 446 · see citing works
Moyal, L., Lerenthal, Y., Gana‐Weisz, M., Mass, G., So, S., Wang, S., Eppink, B., Chung, Y. M., Shalev, G., Shema, E., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.02.015 · Cited by 402 · see citing works
Mallette, F. A., Mattiroli, F., Cui, G., Young, L. C., Hendzel, M. J., Mer, G., Sixma, T. K., & Richard, S. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.47 · Cited by 358 · see citing works
Non-canonical inhibition of DNA damage-dependent ubiquitination by OTUB1
Nakada, S., Tai, I., Panier, S., Al-Hakim, A., Iemura, S.-I., Juang, Y.-C., O’Donnell, L., Kumakubo, A., Munro, M., Sicheri, F., et al. (2010) · Nature · doi:10.1038/nature09297 · Cited by 357 · see citing works
The AAA-ATPase VCP/p97 promotes 53BP1 recruitment by removing L3MBTL1 from DNA double-strand breaks
Ács, K., Luijsterburg, M. S., Ackermann, L., Salomons, F. A., Hoppe, T., & Dantuma, N. P. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2188 · Cited by 280 · see citing works
HERC2 coordinates ubiquitin-dependent assembly of DNA repair factors on damaged chromosomes
Bekker‐Jensen, S., Danielsen, J. M. R., Fugger, K., Gromova, I., Nerstedt, A., Lukas, C., Bártek, J., Lukas, J., & Mailand, N. (2009) · Nature Cell Biology · doi:10.1038/ncb2008 · Cited by 277 · see citing works
Ubiquitin signalling in DNA replication and repair
Ulrich, H. D., & Walden, H. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2921 · Cited by 272 · see citing works
The ubiquitin-selective segregase VCP/p97 orchestrates the response to DNA double-strand breaks
Meerang, M., Ritz, D., Paliwal, S., Garajovà, Z., Bosshard, M., Mailand, N., Janščák, P., Hübscher, U., Meyer, H. H., & Ramadan, K. (2011) · Nature Cell Biology · doi:10.1038/ncb2367 · Cited by 258 · see citing works
The E3 ligase RNF8 regulates KU80 removal and NHEJ repair
Feng, L., & Chen, J. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2211 · Cited by 245 · see citing works
Self-citationThe ubiquitous role of ubiquitin in the DNA damage response
Al-Hakim, A., Escribano‐Diaz, C., Landry, M.-C., O’Donnell, L., Panier, S., Szilard, R. K., & Durocher, D. (2010) · DNA repair · doi:10.1016/j.dnarep.2010.09.011 · Cited by 224 · see citing works
Regulatory ubiquitylation in response to DNA double-strand breaks
Panier, S., & Durocher, D. (2009) · DNA repair · doi:10.1016/j.dnarep.2009.01.013 · Cited by 193 · see citing works
RIDDLE immunodeficiency syndrome is linked to defects in 53BP1-mediated DNA damage signaling
Stewart, G. S., Stanković, T., Byrd, P. J., Wechsler, T., Miller, E. S., Huissoon, A., Drayson, M. T., West, S. C., Elledge, S. J., & Taylor, A. M. R. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0708408104 · Cited by 183 · see citing works
Poulsen, M., Lukas, C., Lukas, J., Bekker-Jensen, S., & Mailand, N. (2012) · Journal of Cell Biology · doi:10.1083/jcb.201109100 · Cited by 146 · see citing works
The ubiquitin landscape at DNA double-strand breaks
Messick, T. E., & Greenberg, R. A. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200908074 · Cited by 130 · see citing works
Assembly of checkpoint and repair machineries at DNA damage sites
Huen, M. S. Y., & Chen, J. (2009) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2009.09.001 · Cited by 116 · see citing works
Self-citationA 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 113 · see citing works
The E3 ubiquitin ligase Rnf8 stabilizes Tpp1 to promote telomere end protection.
Rai, R., Li, J.-M., Zheng, H., Lok, G. T.-M., Deng, Y., Huen, M. S.-Y., Chen, J., Jin, J., & Chang, S. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2172 · Cited by 88 · see citing works
Self-citationDevgan, S. S., Sanal, Ö., Doil, C., Nakamura, K., Nahas, S., Pettijohn, K. J., Bártek, J., Lukas, C., Lukáš, J., & Gatti, R. A. (2011) · Cell Death and Differentiation · doi:10.1038/cdd.2011.18 · Cited by 88 · see citing works
The RNF8/RNF168 ubiquitin ligase cascade facilitates class switch recombination
Ramachandran, S., Chahwan, R., Nepal, R. M., Frieder, D., Panier, S., Roa, S., Zaheen, A., Durocher, D., Scharff, M. D., & Martín, A. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0913790107 · Cited by 85 · see citing works
Bohgaki, T., Bohgaki, M., Cardoso, R., Panier, S., Zeegers, D., Li, L., Stewart, G. S., Sanchez, O. H., Hande, M. P., Durocher, D., et al. (2011) · PLoS Genetics · doi:10.1371/journal.pgen.1001381 · Cited by 83 · see citing works
Huen, M. S. Y., Huang, J., Leung, J. W. C., Sy, S. M.-H., Leung, K. M., Ching, Y.-P., Tsao, S. W., & Chen, J. (2010) · Molecular Cell · doi:10.1016/j.molcel.2009.12.040 · Cited by 73 · see citing works
Self-citationUMI, a Novel RNF168 Ubiquitin Binding Domain Involved in the DNA Damage Signaling Pathway
Pinato, S., Gatti, M., Scandiuzzi, C., Confalonieri, S., & Penengo, L. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.00818-10 · Cited by 63 · see citing works
Critical Roles of Ring Finger Protein RNF8 in Replication Stress Responses
Sy, S. M.-H., Jiang, J., Dong, S.-S., Lok, G. T.-M., Wu, J., Cai, H. “., Yeung, E. S. L., Huang, J., Chen, J., Deng, Y., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.232041 · Cited by 34 · see citing works
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
Double-strand break repair: 53BP1 comes into focus
Panier, S., & Boulton, S. J. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3719 · Cited by 1,090 · see citing works
Regulation of DNA double-strand break repair by ubiquitin and ubiquitin-like modifiers
Schwertman, P., Bekker‐Jensen, S., & Mailand, N. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.58 · Cited by 354 · see citing works
DNA Damage Response: Three Levels of DNA Repair Regulation
Sirbu, B. M., & Cortez, D. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a012724 · Cited by 272 · see citing works
Histone Ubiquitination: An Integrative Signaling Platform in Genome Stability
Mattiroli, F., & Penengo, L. (2021) · Trends in Genetics · doi:10.1016/j.tig.2020.12.005 · Cited by 240 · see citing works
RNF168 Promotes Noncanonical K27 Ubiquitination to Signal DNA Damage
Gatti, M., Pinato, S., Maiolica, A., Rocchio, F., Prato, M. G., Aebersold, R. H., & Penengo, L. (2015) · Cell Reports · doi:10.1016/j.celrep.2014.12.021 · Cited by 220 · see citing works
Spatiotemporal regulation of posttranslational modifications in the DNA damage response
Dantuma, N. P., & van Attikum, H. (2015) · The EMBO Journal · doi:10.15252/embj.201592595 · Cited by 200 · see citing works
Push back to respond better: regulatory inhibition of the DNA double-strand break response
Panier, S., & Durocher, D. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3659 · Cited by 168 · see citing works
Ubiquitylation, neddylation and the DNA damage response
Brown, J. S., & Jackson, S. P. (2015) · Open Biology · doi:10.1098/rsob.150018 · Cited by 147 · see citing works
Molecular Mechanisms of Arsenic-Induced Disruption of DNA Repair
Tam, L. M., Price, N. E., & Wang, Y. (2020) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.9b00464 · Cited by 153 · see citing works
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 125 · see citing works
USP7 Is a Master Regulator of Genome Stability
Valles, G. J., Bezsonova, I., Woodgate, R., & Ashton, N. W. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00717 · Cited by 114 · see citing works
Hu, Q., Botuyan, M. V., Cui, G., Zhao, D., & Mer, G. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.04.009 · Cited by 94 · see citing works
CHD chromatin remodelling enzymes and the DNA damage response
Stanley, F. K. T., Moore, S., & Goodarzi, A. A. (2013) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2013.07.008 · Cited by 74 · see citing works
Immediate-Early, Early, and Late Responses to DNA Double Stranded Breaks
Kieffer, S., & Lowndes, N. (2022) · Frontiers in Genetics · doi:10.3389/fgene.2022.793884 · Cited by 63 · see citing works
The ubiquitin specific protease USP34 promotes ubiquitin signaling at DNA double-strand breaks
Sy, S. M.-H., Jiang, J., O, W. S., Deng, Y., & Huen, M. S. Y. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt622 · Cited by 68 · see citing works
Self-citationRNF169 limits 53BP1 deposition at DSBs to stimulate single-strand annealing repair
An, L., Dong, C., Li, J., Chen, J., Yuan, J., Huang, J., Chan, K. M., Yu, C., & Huen, M. S. Y. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1804823115 · Cited by 69 · see citing works
Self-citationPinder, J. B., Attwood, K. M., & Dellaire, G. (2013) · Frontiers in Genetics · doi:10.3389/fgene.2013.00045 · Cited by 61 · see citing works
Acetylation of 53BP1 dictates the DNA double strand break repair pathway
Guo, X. Y., Bai, Y., Zhao, M., Zhou, M., Shen, Q., Yun, C., Zhang, H., Zhu, W., & Wang, J. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx1208 · Cited by 61 · see citing works
Dual-utility NLS drives RNF169-dependent DNA damage responses
An, L., Jiang, Y., Ng, H. H. W., Man, E. P. S., Chen, J., Khoo, U., Gong, Q., & Huen, M. S. Y. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1616602114 · Cited by 60 · see citing works
Self-citationReading chromatin signatures after DNA double-strand breaks
Wilson, M. D., & Durocher, D. (2017) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2016.0280 · Cited by 58 · see citing works
Menon, V., Ananthapadmanabhan, V., Swanson, S. K., Saini, S., Sesay, F. F., Yakovlev, V. A., Florens, L. A., DeCaprio, J. A., Washburn, M. P., Dozmorov, M. G., et al. (2019) · Cell Cycle · doi:10.1080/15384101.2019.1577525 · Cited by 53 · see citing works
Kitevski-LeBlanc, J. L., Fradet‐Turcotte, A., Kukić, P., Wilson, M. D., Portella, G., Yuwen, T., Panier, S., Duan, S., Canny, M. D., van Ingen, H., et al. (2017) · eLife · doi:10.7554/elife.23872 · Cited by 57 · see citing works
Baranes‐Bachar, K., Levy‐Barda, A., Oehler, J., Reid, D. A., Soria‐Bretones, I., Voss, T. C., Chung, D., Park, Y., Liu, C., Yoon, J., et al. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.02.002 · Cited by 55 · see citing works
Moving Mountains—The BRCA1 Promotion of DNA Resection
Densham, R. M., & Morris, J. R. (2019) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2019.00079 · Cited by 53 · see citing works
Mechanism of 53BP1 activity regulation by RNA-binding TIRR and a designer protein
Botuyan, M. V., Cui, G., Drané, P., Oliveira, C., Detappe, A., Brault, M. E., Parnandi, N., Chaubey, S., Thompson, J. R., Bragantini, B., et al. (2018) · Nature Structural & Molecular Biology · doi:10.1038/s41594-018-0083-z · Cited by 51 · see citing works
To spread or not to spread—chromatin modifications in response to DNA damage
Altmeyer, M., & Lukas, J. (2013) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2012.11.001 · Cited by 49 · see citing works
Writers, Readers, and Erasers of Histone Ubiquitylation in DNA Double-Strand Break Repair
Smeenk, G., & Mailand, N. (2016) · Frontiers in Genetics · doi:10.3389/fgene.2016.00122 · Cited by 47 · see citing works
Roewenstrunk, J., Vona, C. D., Chen, J., Borràs, E., Dong, C., Arató, K., Sabidó, E., Huen, M. S. Y., & de la Luna, S. (2019) · Scientific Reports · doi:10.1038/s41598-019-42445-x · Cited by 48 · see citing works
Self-citationHistone modifications in DNA damage response
Cao, L., Shen, C., & Zhu, W. (2016) · Science China Life Sciences · doi:10.1007/s11427-016-5011-z · Cited by 45 · see citing works
An LTR retrotransposon‐derived lncRNA interacts with RNF169 to promote homologous recombination
Deng, B., Xu, W., Wang, Z., Liu, C., Lin, P., Li, B., Huang, Q., Yang, J., Zhou, H., & Qu, L. (2019) · The EMBO Reports · doi:10.15252/embr.201847650 · Cited by 40 · see citing works
Ubiquitin and ubiquitin-like molecules in DNA double strand break repair
Yu, J., Qin, B., & Lou, Z. (2020) · Cell & Bioscience · doi:10.1186/s13578-020-0380-1 · Cited by 33 · see citing works
USP19 deubiquitinates HDAC1/2 to regulate DNA damage repair and control chromosomal stability
Wu, M., Tu, H.-Q., Chang, Y., Tan, B., Wang, G., Zhou, J., Wang, L., Mu, R., & Zhang, W. (2016) · Oncotarget · doi:10.18632/oncotarget.11116 · Cited by 36 · see citing works
It takes two to tango: Ubiquitin and SUMO in the DNA damage response
Bologna, S., & Ferrari, S. M. (2013) · Frontiers in Genetics · doi:10.3389/fgene.2013.00106 · Cited by 32 · see citing works
Takahashi, T. S., Hirade, Y., Toma, A., Sato, Y., Yamagata, A., Goto‐Ito, S., Tomita, A., Nakada, S., & Fukai, S. (2018) · Nature Communications · doi:10.1038/s41467-017-02345-y · Cited by 32 · see citing works
RNF126 Quenches RNF168 Function in the DNA Damage Response
Lian-zhong, Z., Wang, Z., Shi, R., Zhu, X., Zhou, J., Peng, B., & Xu, X. (2018) · Genomics Proteomics & Bioinformatics · doi:10.1016/j.gpb.2018.07.004 · Cited by 30 · see citing works
Mechanisms of RNF168 nucleosome recognition and ubiquitylation
Hu, Q., Zhao, D., Cui, G., Bhandari, J., Thompson, J. R., Botuyan, M. V., & Mer, G. (2024) · Molecular Cell · doi:10.1016/j.molcel.2023.12.036 · Cited by 28 · see citing works
USP39 promotes non-homologous end-joining repair by poly(ADP-ribose)-induced liquid demixing
Kim, J. J., Lee, S. Y., Hwang, Y., Kim, S., Chung, J. M., Park, S., Yoon, J., Yun, H., Ji, J., Chae, S., et al. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkab892 · Cited by 28 · see citing works
A small ubiquitin binding domain inhibits ubiquitin-dependent protein recruitment to DNA repair foci
Helchowski, C. M., Skow, L., Roberts, K. H., Chute, C. L., & Canman, C. E. (2013) · Cell Cycle · doi:10.4161/cc.26640 · Cited by 26 · see citing works
A DYRK1B-dependent pathway suppresses rDNA transcription in response to DNA damage
Dong, C., An, L., Yu, C., & Huen, M. S. Y. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkaa1290 · Cited by 25 · see citing works
Self-citationMoquin, D., Genois, M., Zhang, J., Ouyang, J., Yadav, T., Buisson, R., Yazinski, S. A., Tan, J. J., Boukhali, M., Gagné, J., et al. (2018) · Genes & Development · doi:10.1101/gad.315978.118 · Cited by 23 · see citing works
Garvin, A. J. (2019) · Biochemical Society Transactions · doi:10.1042/bst20190534 · Cited by 22 · see citing works
Insights from the protein interaction Universe of the multifunctional “Goldilocks” kinase DYRK1A
Ananthapadmanabhan, V., Shows, K. H., DICKINSON, A. J. G., & Litovchick, L. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1277537 · Cited by 23 · see citing works
Structural basis for role of ring finger protein RNF168 RING domain
Zhang, X., Chen, J., Wu, M., Wu, H., Arokiaraj, A. W. R., Wang, C., Zhang, W., Tao, Y., Huen, M. S. Y., & Zang, J. (2013) · Cell Cycle · doi:10.4161/cc.23104 · Cited by 22 · see citing works
Self-citationCircGNB1 drives osteoarthritis pathogenesis by inducing oxidative stress in chondrocytes
Liang, Y., Shen, L., Ni, W., Ding, Y., Yang, W., Gu, T., Zhang, C., Yik, J. H. N., Haudenschild, D. R., Fan, S., et al. (2023) · Clinical and Translational Medicine · doi:10.1002/ctm2.1358 · Cited by 21 · see citing works
FOXK1 Participates in DNA Damage Response by Controlling 53BP1 Function
Tang, M., Feng, X., Pei, G., Srivastava, M., Wang, C., Chen, Z., Li, S., Zhang, H., Zhao, Z., Li, X., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.108018 · Cited by 20 · see citing works
Self-citationUbiquitylation in DNA double-strand break repair
Tang, M., Li, S., & Chen, J. (2021) · DNA repair · doi:10.1016/j.dnarep.2021.103129 · Cited by 22 · see citing works
Self-citationBCL10 regulates RNF8/RNF168-mediated ubiquitination in the DNA damage response
Zhao, H., Zhu, M., Dou, G., Zhao, H., Zhu, B., Li, J., Liao, J., & Xu, X. (2014) · Cell Cycle · doi:10.4161/cc.28707 · Cited by 17 · see citing works
Chromatin Ubiquitination Guides DNA Double Strand Break Signaling and Repair
Kolobynina, K. G., Rapp, A. W., & Cardoso, M. C. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.928113 · Cited by 17 · see citing works
Han, D., Liang, J., Lu, Y., Xu, L., Miao, S., Lu, L., Song, W., & Wang, L. (2016) · PLoS ONE · doi:10.1371/journal.pone.0155476 · Cited by 13 · see citing works
Guarding against Collateral Damage during Chromatin Transactions
Altmeyer, M., & Lukas, J. (2013) · Cell · doi:10.1016/j.cell.2013.05.044 · Cited by 13 · see citing works
Ubiquitin E3 ligases in cancer: somatic mutation and amplification
Jo, E.-H., Kim, M., Lee, H.-J., & Park, H.-S. (2023) · BMB Reports · doi:10.5483/bmbrep.2023-0037 · Cited by 12 · see citing works
Dantuma, N. P., & Pfeiffer, A. (2016) · Frontiers in Genetics · doi:10.3389/fgene.2016.00058 · Cited by 11 · see citing works
DoUBLing up: ubiquitin and ubiquitin-like proteases in genome stability
Foster, B. M., Wang, Z., & Schmidt, C. K. (2024) · Biochemical Journal · doi:10.1042/bcj20230284 · Cited by 10 · see citing works
Eukaryotic DNA damage responses: Homologous recombination factors and ubiquitin modification
Lee, N. S., Kim, S.-M., Jung, Y. W., & Kim, H. (2017) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2017.04.003 · Cited by 8 · see citing works
UBA80 and UBA52 fine-tune RNF168-dependent histone ubiquitination and DNA repair
Lee, S.-O., Kelliher, J. L., Song, W., Tengler, K., Sarkar, A., Dray, E. V., & Leung, J. W. C. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.105043 · Cited by 10 · see citing works
Mok, M. T. S., Cheng, A. S. L., & Henderson, B. R. (2014) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2014.09.027 · Cited by 10 · see citing works
Wang, J., Chen, H., Deng, Q., Chen, Y., Wang, Z., Yan, Z., Wang, Y., Tang, H.-X., Liang, H., & Jiang, Y. (2023) · Frontiers in Genetics · doi:10.3389/fgene.2022.1022626 · Cited by 9 · see citing works
Nucleolar residence of the seckel syndrome protein TRAIP is coupled to ribosomal DNA transcription
Chen, Y., Li, J., Cao, F., Lam, J., Cheng, C. C., Yu, C., & Huen, M. S. Y. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky775 · Cited by 9 · see citing works
Self-citationRing finger protein 219 regulates inflammatory responses by stabilizing sirtuin 1
Hwang, J. S., Kim, E., Hur, J., Yoon, T. J., & Seo, H. G. (2020) · British Journal of Pharmacology · doi:10.1111/bph.15060 · Cited by 8 · see citing works
Ubiquitin and the DNA double-strand break repair pathway
Nowsheen, S., Deng, M., & Lou, Z. (2019) · Genome Instability & Disease · doi:10.1007/s42764-019-00007-5 · Cited by 8 · see citing works
Chauhan, A. S., Mackintosh, M. J. W., Cassar, J., Lanz, A. J., Jamshad, M., Mackay, H. L., Garvin, A. J., Walker, A. K., Jhujh, S. S., Carlomagno, T., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-56974-9 · Cited by 8 · see citing works
Reilly, N. M., Yard, B. D., & Pittman, D. L. (2019) · Methods in molecular biology · doi:10.1007/978-1-4939-9500-4_1 · Cited by 7 · see citing works
Hall, T. O., Stanaway, I. B., Carrell, D., Carroll, R. J., Denny, J. C., Hakonarson, H. H., Larson, E. B., Mentch, F. D., Peissig, P. L., Pendergrass, S. A., et al. (2018) · Genes and Immunity · doi:10.1038/s41435-018-0051-y · Cited by 7 · see citing works
Ghosh, S., Bartenhagen, C., Okpanyi, V., Gombert, M., Binder, V., Teigler‐Schlegel, A., Bradtke, J., Röttgers, S., Dugas, M., & Borkhardt, A. (2013) · Leukemia · doi:10.1038/leu.2013.1 · Cited by 5 · see citing works
Chang, Y., Sun, Z., & Xu, M. (2025) · World Journal of Surgical Oncology · doi:10.1186/s12957-025-04036-1 · Cited by 1 · see citing works
E3 Ubiquitin Ligases as Molecular Machines and Platforms for Drug Development
Ioris, R. M., Ferris, K., & D’Angiolella, V. (2022) · Wiley eBooks · doi:10.1002/9783527836208.ch3 · Cited by 1 · see citing works
Investigation of Ring Finger Protein 8 in Mammalian Physiology and Pathogenesis
Li, L. (2015) · TSpace (University of Toronto)
Barnes, M. R. (2020) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.737173646.793569381
Stabilité du génome et rôle des INGs dans la réponse aux dommages de l'ADN
Mouche, A. (2017) · theses.fr (ABES) · doi:10.70675/2eac02ceze1a0z4c25z9effza47f3d916ad9
Cristini, A. (2015) · theses.fr (ABES) · doi:10.70675/89719cadza51cz4509zbd9fz3da99c280491
- Authors
- Chen, J., Feng, W., Jiang, J., Deng, Y., & Huen, M. S. Y.
- Affiliations
- University of Hong Kong (HK)
- South China Agricultural University (CN)
- Corresponding author
- Deng, Yiqun
- Huen, Michael S.Y.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2012-08
- Volume
- 287
- Issue
- 33
- Pages
- 27715-27722
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC3431699
- OpenAlex
- W1976678739
- Cited by
- 72
- References
- 31
- Citations by year
- 2025: 2 · 2024: 2 · 2023: 5 · 2022: 3 · 2021: 4 · 2020: 6 · 2019: 7 · 2018: 8 · 2017: 7 · 2016: 7 · 2015: 5 · 2014: 3 · 2013: 13
- FWCI
- 2.70
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- The HKU Scholars Hub (University of Hong Kong) (submittedVersion)
- Funders
- National Key Research and Development Program of China
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
- Keywords
- RNF8, RNF168, E3 ubiquitin ligase, DNA double-strand breaks, DNA damage signaling, ubiquitination, 53BP1, genome stability
- MeSH terms
- Cell Line, DNA-Binding Proteins, Humans, Signal Transduction, Ubiquitin, Genomic Instability, Ubiquitin-Protein Ligases, DNA Breaks, Double-Stranded, Ubiquitination
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
