RNF4, a SUMO-targeted ubiquitin E3 ligase, promotes DNA double-strand break repair

The DNA-damage response in human biology and disease

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ATM and ATR Substrate Analysis Reveals Extensive Protein Networks Responsive to DNA Damage

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SUMO

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Human CtIP promotes DNA end resection

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RNF8 Ubiquitylates Histones at DNA Double-Strand Breaks and Promotes Assembly of Repair Proteins

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MDC1 Directly Binds Phosphorylated Histone H2AX to Regulate Cellular Responses to DNA Double-Strand Breaks

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DNA damage emergency: cellular garbage disposal to the rescue?

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F-box only and CUE proteins are crucial ubiquitination-associated components for conidiation and pathogenicity in the rice blast fungus, Magnaporthe oryzae

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RNF4 Regulates the BLM Helicase in Recovery From Replication Fork Collapse

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USP7/HAUSP: A SUMO deubiquitinase at the heart of DNA replication

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Progress in the Discovery of Small Molecule Modulators of DeSUMOylation

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Functional 3D architecture in an intrinsically disordered E3 ligase domain facilitates ubiquitin transfer

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Microarray screening reveals two non-conventional SUMO-binding modules linked to DNA repair by non-homologous end-joining

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The Biology of SUMO-Targeted Ubiquitin Ligases in Drosophila Development, Immunity, and Cancer

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Knockdown of endogenous RNF4 exacerbates ischaemia‐induced cardiomyocyte apoptosis in mice

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SUMO ‐targeted ubiquitin ligase RNF 4 plays a critical role in preventing chromosome loss

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Slx8 Removes Pli1-Dependent Protein-SUMO Conjugates Including SUMOylated Topoisomerase I to Promote Genome Stability

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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

Circadian PERIOD proteins regulate TC-DSB repair through anchoring to the nuclear envelope

Bozec, B. L., Guitton-Sert, L., Collins, S., Finoux, A.-L., Payrault, C., Guillou, E., Aguirrebengoa, M., Dougados, V., Jouffret, V., Frison, J., et al. (2025) · Molecular Cell · doi:10.1016/j.molcel.2025.10.027 · Cited by 17

Mitotic and Meiotic Functions for the SUMOylation Pathway in the Caenorhabditis elegans Germline

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Ubiquitylation-Mediated Fine-Tuning of DNA Double-Strand Break Repair

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SUMO: A Swiss Army Knife for Eukaryotic Topoisomerases

Sun, Y., Nitiss, J. L., & Pommier, Y. G. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.871161 · Cited by 16

PIAS3 promotes homology-directed repair and distal non-homologous end joining

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RNF4-mediated SUMOylation is essential for NDRG2 suppression of lung adenocarcinoma

Tantai, J., Pan, X., & Hu, D. (2016) · Oncotarget · doi:10.18632/oncotarget.8663 · Cited by 16

The Molecular Interface Between the SUMO and Ubiquitin Systems

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DNA binding by the MATα2 transcription factor controls its access to alternative ubiquitin-modification pathways

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The E3 Ubiquitin-Protein Ligase RNF4 Promotes TNF-α-Induced Cell Death Triggered by RIPK1

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A Lysine Desert Protects a Novel Domain in the Slx5-Slx8 SUMO Targeted Ub Ligase To Maintain Sumoylation Levels in Saccharomyces cerevisiae

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RNF4-mediated SUMO-targeted ubiquitination relieves PARIS/ZNF746-mediated transcriptional repression

Nishida, T., & Yamada, Y. (2020) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2020.03.063 · Cited by 14

Exploring the RING-Catalyzed Ubiquitin Transfer Mechanism by MD and QM/MM Calculations

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RNF4 sustains Myc-driven tumorigenesis by facilitating DNA replication

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To Ub or not to Ub: The epic dilemma of histones that regulate gene expression and epigenetic cross-talk

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SUMO4 promotes SUMO deconjugation required for DNA double-strand-break repair

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VCP maintains nuclear size by regulating the DNA damage-associated MDC1–p53–autophagy axis in Drosophila

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STUbLs in chromatin and genome stability

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Revisiting regulatory roles of replication protein A in plant DNA metabolism

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Replication protein A as a major eukaryotic single-stranded DNA-binding protein and its role in DNA repair

Krasikova, Y. S., Rechkunova, N. I., & Lavrik, O. I. (2016) · Molecular Biology · doi:10.1134/s0026893316030080 · Cited by 13

Preserving genome integrity: The vital role of SUMO-targeted ubiquitin ligases

Han, J., Mu, Y., & Huang, J. (2023) · Cell Insight · doi:10.1016/j.cellin.2023.100128 · Cited by 11

PRMT1 arginine methyltransferase accumulates in cytoplasmic bodies that respond to selective inhibition and DNA damage

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Loss of ubiquitin E2 Ube2w rescues hypersensitivity of Rnf4 mutant cells to DNA damage

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Attenuation of the ubiquitin conjugate DNA damage signal by the proteasomal DUB POH1

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How SUMOylation Fine-Tunes the Fanconi Anemia DNA Repair Pathway

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Novel insights into the impact of the SUMOylation pathway in hematological malignancies (Review)

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RNF4 silencing induces cell growth arrest and DNA damage by promoting nuclear targeting of p62 in hepatocellular carcinoma

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Real Estate in the DNA Damage Response: Ubiquitin and SUMO Ligases Home in on DNA Double-Strand Breaks

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Effect of ionizing radiation exposure on Trypanosoma cruzi ubiquitin-proteasome system

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Arsenic trioxide and angiotensin II have inhibitory effects on HERG protein expression: Evidence for the role of PML SUMOylation

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Eukaryotic DNA damage responses: Homologous recombination factors and ubiquitin modification

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DNA Damage Induction Alters the Expression of Ubiquitin and SUMO Regulators in Preimplantation Stage Pig Embryos

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RNA methylation, homologous recombination repair and therapeutic resistance

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The Intriguing Mystery of RPA Phosphorylation in DNA Double-Strand Break Repair

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Legionella pneumophila exploits the endo-lysosomal network for phagosome biogenesis by co-opting SUMOylated Rab7

Li, C., Fu, J., Shao, S., & Luo, Z. (2024) · PLoS Pathogens · doi:10.1371/journal.ppat.1011783 · Cited by 12

Репликативный белок А – ключевой белок, связывающий одноцепочечную ДНК в клетках эукариот, и его роль в репарации ДНК

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The SUMO-targeted ubiquitin ligase RNF4 localizes to etoposide-exposed mitotic chromosomes: Implication for a novel DNA damage response during mitosis

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Balancing act: To be, or not to be ubiquitylated

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On‐site remodeling at chromatin: How multiprotein complexes are rebuilt during DNA repair and transcriptional activation

Papadopoulou, T., & Richly, H. (2016) · BioEssays · doi:10.1002/bies.201600094 · Cited by 10

RNF4 and USP7 cooperate in ubiquitin-regulated steps of DNA replication

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Poly(ADP-ribosyl)ation temporally confines SUMO-dependent ataxin-3 recruitment to control DNA double-strand break repair

Pfeiffer, A., Herzog, L. K., Luijsterburg, M. S., Shah, R. G., Rother, M. B., Stoy, H., Kühbacher, U., van Attikum, H., Shah, G. M., & Dantuma, N. P. (2021) · Journal of Cell Science · doi:10.1242/jcs.247809 · Cited by 9

The role and mechanism of SUMO modification in liver disease

Li, M., Zhang, J., Li, Z., Zhou, X., Qian, S., Tay, L. J., Zhang, Z., Yang, F., & Huang, Y. (2024) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2024.116898 · Cited by 9

DNA damage-induced proteasome phosphorylation controls substrate recognition and facilitates DNA repair

Zhang, X., Zhu, T., Li, X., Zhao, H., Lin, S., Huang, J., Yang, B., & Guo, X. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2321204121 · Cited by 8

RNF4 regulates zebrafish granulopoiesis through the DNMT1‐C/EBPα axis

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Methods to analyze STUbL activity

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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

PIN1-SUMO2/3 motif suppresses excessive RNF168 chromatin accumulation and ubiquitin signaling to promote IR resistance

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

Determining the Fate of Neurons in SCA3: ATX3, a Rising Decision Maker in Response to DNA Stresses and Beyond

Tu, Y., Li, X., Zhu, X., Liu, X., Guo, C., Jia, D., & Tang, T.-S. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.619911 · Cited by 8

Roles of the SUMO-related enzymes, PIAS1, PIAS4, and RNF4, in DNA double-strand break repair by homologous recombination

Han, M. M., Hirakawa, M., Yamauchi, M., & Matsuda, N. (2021) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2021.12.099 · Cited by 7

Direct binding of RNF8 to SUMO2/3 promotes cell survival following DNA damage

Liang, L., Zhang, Z., Li, J., Wu, J., Wang, L., Huang, W., & Gao, S. (2017) · Molecular Medicine Reports · doi:10.3892/mmr.2017.7624 · Cited by 7

Multiple interaction nodes define the postreplication repair response to UV‐induced DNA damage that is defective in melanomas and correlated with UV signature mutation load

Pavey, S. J., Pinder, A., Fernando, W., D’Arcy, N., Matigian, N., Škalamera, D., Cao, K. L., Loo, D., Hill, M. M. C., Stark, M. S., et al. (2019) · Molecular Oncology · doi:10.1002/1878-0261.12601 · Cited by 6

Targeting ATR-CHK1 and ATM-CHK2 Axes in Pancreatic Cancer—A Comprehensive Review of Literature

Kciuk, M., Wanke, K., Marciniak, B., Kołat, D., Aleksandrowicz, M., Mujwar, S., Ainane, T., & Kontek, R. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27031152 · Cited by 7

Proteasomal control of transcription factors: mechanisms, regulation and dysregulation

Larsen, F. B., Kragelund, B. B., Lindorff‐Larsen, K., Heidarsson, P. O., & Hartmann‐Petersen, R. (2026) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-026-06103-6 · Cited by 6

Quantitative Fitness Analysis Identifies exo1∆ and Other Suppressors or Enhancers of Telomere Defects in Schizosaccharomyces pombe

Narayanan, S., Dubarry, M., Lawless, C., Banks, A. P., Wilkinson, D. J., Whitehall, S. K., & Lydall, D. A. (2015) · PLoS ONE · doi:10.1371/journal.pone.0132240 · Cited by 6

WIP1 Contributes to the Adaptation of Fanconi Anemia Cells to DNA Damage as Determined by the Regulatory Network of the Fanconi Anemia and Checkpoint Recovery Pathways

Rodríguez, A., Naveja, J. J., Torres, L., Teresa, B. G., Juárez, U., Ayala-Zambrano, C., Azpeitia, E. M., Mendoza, L., & Frı́as, S. (2019) · Frontiers in Genetics · doi:10.3389/fgene.2019.00411 · Cited by 7

CENP-B dynamics at centromeres is regulated by a SUMOylation/ubiquitination and proteasomal-dependent degradation mechanism involving the SUMO-targeted ubiquitin E3 ligase RNF4Preprint

Maalouf, J. E., Texier, P., Erliandri, I., Cohen, C., Corpet, A., Catez, F., Boutell, C., & Lomonte, P. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/245597 · Cited by 6

Legionella pneumophila exploits the endo-lysosomal network for phagosome biogenesis by co-opting SUMOylated Rab7Preprint

Li, C., Fu, J., Shao, S., & Luo, Z. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.10.31.564884 · Cited by 6

Multifaceted roles of SUMO in DNA metabolism

Thu, Y. M. (2024) · Nucleus · doi:10.1080/19491034.2024.2398450 · Cited by 5

mRNA markers associated with malignant pleural effusion

Hsu, S., Chang, S., Hwang, Y., Terng, H.-J., Tsai, C., Shen, C., Huang, S. K., & Chian, C. (2023) · Scientific Reports · doi:10.1038/s41598-023-32872-2 · Cited by 5

Role of Ionizing Radiation in Shaping the Complex Multi-Layered Epigenome

Rübe, C. E., Al‐razaq, M. A. A., Meier, C., Hecht, M., & Rübe, C. (2025) · Epigenomes · doi:10.3390/epigenomes9030029 · Cited by 5

RNF4 interacts with multiSUMOylated ETV4

Aguilar-Martínez, E., Guo, B., & Sharrocks, A. D. (2017) · Wellcome Open Research · doi:10.12688/wellcomeopenres.9935.2 · Cited by 4

Cysteine-reactive covalent chloro-N-acetamide ligands induce ferroptosis mediated cell death

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The role of HECT-type E3 ubiquitin ligases in DNA damage response and repair

Giovannini, S., Fiorilli, C., Moriconi, V., Shi, Y., Candi, E., Melino, G., & Bernassola, F. (2025) · Cell Death Discovery · doi:10.1038/s41420-025-02911-0 · Cited by 3

Systematic comparison of differential expression networks in MTB mono-, HIV mono- and MTB/HIV co-infections for drug repurposing

Jiang, Y., Zhang, J., & Liu, R. (2022) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1010744 · Cited by 3

Integrated analysis and validation of the TRIM28-H2AX-CDK4 diagnostic model assists to predict the progression of HCC

Tian, Q., Lu, G., Ma, Y., Ma, L., Shang, Y., Guo, N., Huang, Y., Zhu, L., & Du, R. (2023) · Aging · doi:10.18632/aging.205137 · Cited by 3

Depletion of UBC9 Causes Nuclear Defects during the Vegetative and Sexual Life Cycles in Tetrahymena thermophila

Yang, Q., Nasir, A. M., Coyne, R. S., & FORNEY, J. D. (2015) · Eukaryotic Cell · doi:10.1128/ec.00115-15 · Cited by 3

RNF4 interacts with multiSUMOylated ETV4

Aguilar-Martínez, E., Guo, B., & Sharrocks, A. D. (2016) · Wellcome Open Research · doi:10.12688/wellcomeopenres.9935.1 · Cited by 3

Phosphorylation of RNF213 by ATM-mediated ubiquitination of RPA1 regulates homologous recombination repair and chemosensitivity

Hu, D., Wu, W., Wu, C., Li, J., Ruan, B., Cheng, H., Jiang, Y., Wang, Y., & Song, Z. (2025) · Cell Death and Disease · doi:10.1038/s41419-025-08041-w · Cited by 2

Chromatin Remodeling in DNA Damage Response and Human Aging

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Pin1-promoted SUMOylation of RNF168 restrains its chromatin accumulationPreprint

Chauhan, A. S., Garvin, A. J., Jamshad, M., & Morris, J. R. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.03.22.485326 · Cited by 2

Recent advances in understanding the molecular mechanisms of SLX4 recruitment in the replication stress response

Okano, T., Takata, M., Fujita, M., & Katsuki, Y. (2025) · DNA repair · doi:10.1016/j.dnarep.2025.103911 · Cited by 1

DNA double strand break repair: a model of specificity and complexity in SUMO signalling

Bhachoo, J. S., & Garvin, A. J. (2025) · Essays in Biochemistry · doi:10.1042/ebc20253043 · Cited by 1

Deciphering the Ubiquitin-like Code of DNA-PK: Mechanisms and Therapeutic Opportunities

Zhao, J., Qin, Z., Hou, J., Lu, M., Guo, J., Wu, J., Wang, C., Zhu, X., & Ma, T. (2026) · Biomolecules · doi:10.3390/biom16040498 · Cited by 1

Allosteric activation of PARP2 self‐ PARylation by SUMO constrains DNA ‐break‐dependent catalytic functions

Shivani, A. P., Milee, M., & Rajakumara, E. (2026) · FEBS Journal · doi:10.1111/febs.70661 · Cited by 1

Rare Germline Variants in DNA Repair Genes Detected in BRCA-Negative Finnish Patients with Early-Onset Breast Cancer

Kurkilahti, V., Rathinakannan, V. S., Nynäs, E., Goel, N., Aittomäki, K., Nevanlinna, H. A., Fey, V., Kankuri‐Tammilehto, M., & Schleutker, J. (2024) · Cancers · doi:10.3390/cancers16172955 · Cited by 2

Fine-tuning of SUMOylation modulates drought tolerancePreprint

Li, X., Zhou, S., Lu, L., Dang, H., Liu, Z., Li, H., Chu, B., Chen, P., Ma, Z., Zhao, S., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.03.29.437542 · Cited by 1

SUMO ylation

Kerscher, O. (2016) · Encyclopedia of Life Sciences · doi:10.1002/9780470015902.a0021849.pub2 · Cited by 1

The effect of Kaposi's sarcoma-associated herpesvirus RTA expression upon the cellular proteome

Wood, J. J. (2013) · White Rose eTheses Online (University of Leeds, The University of Sheffield, University of York)

SUMO-1 conjugation in normal and stress conditions in vivo

Mikkonen, L. (2013) · Työväentutkimus Vuosikirja

Characterisation of two deubiquitinating enzymes in the DNA damage response and replication

Stone, H. R. (2015) · University of Birmingham Institutional Research Archive (University of Birmingham)

Characterization of the Role of the Phosphatase and Tensin Homolog, PTEN, in DNA Crosslink Repair

Vuono, E. A. (2016) · doi:10.23860/diss-vuono-elizabeth-2016

A Genome-scale RNA Interference Screen Identifies Novel Regulators of DNA Double-strand Break Repair

Young, J. T. F. (2016) · TSpace (University of Toronto)

Cyclin E1 as a therapeutic target in high grade serous ovarian cancer

Au‐Yeung, G. (2017) · Minerva Access (University of Melbourne)

Ubiquitin, SUMO and PAR : deciphering recruitment signals at DNA damage sites

Pfeiffer, A. (2018) · Figshare

Determining xE2-xE3 Pair of RNF38 by Phage Display for Orthogonal Ubiquitin Transfer

Rios, N. (2022) · Digital Archive @ GSU · doi:10.57709/12019049

Investigation into the functions of sumoylation in yeast

Lewis, C. M. (2017)

Characterizing the Role of the DNA Damage Response in Class switch recombination

Ramachandran, S. (2014) · TSpace (University of Toronto)

うつ病とカテコラミン,セロトニン (脳の生化学と臨床(特集)) -- (中枢神経疾患の病態生化学)

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Progress in the Discovery of Small Molecule Modulators of DeSUMOylation

Shiyao, C., Dong, D., Xin, W., & Zhou, H. (2019) · Caister Academic Press eBooks · doi:10.21775/9781912530120.04

RNF4 is required for DNA double-strand break repair in vivo

Vyas, R., Kumar, R., Clermont, F. F., Helfricht, A., Kalev, P., Sotiropoulou, P., Hendriks, I. A., Radaelli, E., Hochepied, T., Blanpain, C., et al. (2012) · Cell Death and Differentiation · doi:10.1038/cdd.2012.145 · Cited by 120

SUMO-targeted ubiquitin E3 ligase RNF4 is required for the response of human cells to DNA damage

Yin, Y., Seifert, A., Chua, J. S., Maure, J.-F., Golebiowski, F., & Hay, R. T. (2012) · Genes & Development · doi:10.1101/gad.189274.112 · Cited by 237

RNF4 interacts with both SUMO and nucleosomes to promote the DNA damage response

Groocock, L., Nie, M., Prudden, J., Moiani, D., Wang, T., Cheltsov, A. V., Rambo, R. P., Arvai, A. S., Hitomi, C., Tainer, J. A., et al. (2014) · EMBO Reports · doi:10.1002/embr.201338369 · Cited by 49

Ataxin‐3 consolidates the MDC1‐dependent DNA double‐strand break response by counteracting the SUMO‐targeted ubiquitin ligase RNF4

Pfeiffer, A., Luijsterburg, M. S., Ács, K., Wiegant, W. W., Helfricht, A., Herzog, L. K., Minoia, M., Böttcher, C., Salomons, F. A., van Attikum, H., et al. (2017) · The EMBO Journal · doi:10.15252/embj.201695151 · Cited by 80

Roles of the SUMO-related enzymes, PIAS1, PIAS4, and RNF4, in DNA double-strand break repair by homologous recombination

Han, M. M., Hirakawa, M., Yamauchi, M., & Matsuda, N. (2021) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2021.12.099 · Cited by 7