Cited by 160DNA Repair MechanismsUbiquitin and proteasome pathwaysNuclear Structure and Function

The DOI matches its Crossref record; 60 of the 60 references it cites were found in a registry or an index.

DNA repair factor XPC is modified by SUMO-1 and ubiquitin following UV irradiation.

Open access

Wang, Q.-E.·2005·Nucleic Acids Research

Open this paper in CoChat — free account Open PDF

Abstract

Nucleotide excision repair (NER) is the major DNA repair process that removes diverse DNA lesions including UV-induced photoproducts. There are more than 20 proteins involved in NER. Among them, XPC is thought to be one of the first proteins to recognize DNA damage during global genomic repair (GGR), a sub-pathway of NER. In order to study the mechanism through which XPC participates in GGR, we investigated the possible modifications of XPC protein upon UV irradiation in mammalian cells. Western blot analysis of cell lysates from UV-irradiated normal human fibroblast, prepared by direct boiling in an SDS lysis buffer, showed several anti-XPC antibody-reactive bands with molecular weight higher than the original XPC protein. The reciprocal immunoprecipitation and siRNA transfection analysis demonstrated that XPC protein is modified by SUMO-1 and ubiquitin. By using several NER-deficient cell lines, we found that DDB2 and XPA are required for UV-induced XPC modifications. Interestingly, both the inactivation of ubiquitylation and the treatment of proteasome inhibitors quantitatively inhibited the UV-induced XPC modifications. Furthermore, XPC protein is degraded significantly following UV irradiation in XP-A cells in which sumoylation of XPC does not occur. Taken together, we conclude that XPC protein is modified by SUMO-1 and ubiquitin following UV irradiation and these modifications require the functions of DDB2 and XPA, as well as the ubiquitin-proteasome system. Our results also suggest that at least one function of UV-induced XPC sumoylation is related to the stabilization of XPC protein.

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

Crossref · 10.1093/nar/gki684

Cites

60 of 60 references verified0 citation errors · 0 not checkable

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?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO
Hoege, C., Pfander, B., Moldovan, G., Pyrowolakis, G., & Jentsch, S. (2002) · Nature · doi:10.1038/nature00991 · Cited by 2,202
Protein Modification by SUMO
Johnson, E. S. (2004) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.011303.074118 · Cited by 1,711
UBIQUITIN-DEPENDENT PROTEIN DEGRADATION
Hochstrasser, M. (1996) · Annual Review of Genetics · doi:10.1146/annurev.genet.30.1.405 · Cited by 1,706
A Small Ubiquitin-Related Polypeptide Involved in Targeting RanGAP1 to Nuclear Pore Complex Protein RanBP2
Mahajan, R. K., Delphin, C., Guan, T., Gerace, L., & Melchior, F. (1997) · Cell · doi:10.1016/s0092-8674(00)81862-0 · Cited by 1,258
A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex.
Matunis, M. J., Coutavas, E. E., & Blobel, G. (1996) · The Journal of Cell Biology · doi:10.1083/jcb.135.6.1457 · Cited by 1,199
Molecular mechanism of nucleotide excision repair
de Laat, W. L., Jaspers, N. G. J., & Hoeijmakers, J. H. J. (1999) · Genes & Development · doi:10.1101/gad.13.7.768 · Cited by 1,122
SUMO-1 Modification of IκBα Inhibits NF-κB Activation
Desterro, J. M. P., Rodríguez, M. S., & Hay, R. T. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80133-1 · Cited by 1,050
Xeroderma Pigmentosum Group C Protein Complex Is the Initiator of Global Genome Nucleotide Excision Repair
Sugasawa, K., Ng, J. M. Y., Masutani, C., Iwai, S., van der Spek, P. J., Eker, A. P. M., Hanaoka, F., Bootsma, D., & Hoeijmakers, J. H. J. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80132-x · Cited by 899
Functional Heterogeneity of Small Ubiquitin-related Protein Modifiers SUMO-1 versus SUMO-2/3
Saitoh, H., & Hinchey, J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.9.6252 · Cited by 897
Mammalian DNA nucleotide excision repair reconstituted with purified protein components
Aboussekhra, A., Biggerstaff, M., Shivji, M. K. K., Vilpo, J. A., Moncollin, V., Podust, V. N., Protić, M., Hübscher, U., Egly, J.-M., & Wood, R. D. (1995) · Cell · doi:10.1016/0092-8674(95)90289-9 · Cited by 837

Flagged first, then by citations

Show all 59 references

Research works printed but not linked: 1

[46]Desterro J.M. Rodriguez M.S. Hay R.T. SUMO-1 modification of IkappaBalpha inhibits NF-kappaB activation Mol. Cell 1998 2 233 239 9734360

Sorted by citations

Understanding nucleotide excision repair and its roles in cancer and ageing
Marteijn, J. A., Lans, H., Vermeulen, W., & Hoeijmakers, J. H. J. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3822 · Cited by 1,192
Principles of ubiquitin and SUMO modifications in DNA repair
Bergink, S., & Jentsch, S. (2009) · Nature · doi:10.1038/nature07963 · Cited by 554
A comprehensive compilation of SUMO proteomics
Hendriks, I. A., & Vertegaal, A. C. O. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.81 · Cited by 514
A Gene Expression Model of Intrinsic Tumor Radiosensitivity: Prediction of Response and Prognosis After Chemoradiation
Eschrich, S. A., Pramana, J., Zhang, H., Zhao, H., Boulware, D., Lee, J.-H., Bloom, G., Rocha-Lima, C., Kelley, S., Calvin, D. P., et al. (2009) · International Journal of Radiation Oncology*Biology*Physics · doi:10.1016/j.ijrobp.2009.06.014 · Cited by 360
The DDB1-CUL4A DDB2 ubiquitin ligase is deficient in xeroderma pigmentosum group E and targets histone H2A at UV-damaged DNA sites
Kapetanaki, M. G., Guerrero‐Santoro, J., Bisi, D. C., Hsieh, C. L., Rapić-Otrin, V., & Levine, A. S. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0511160103 · Cited by 323
Circadian clock control of the cellular response to DNA damage
Sancar, A., Lindsey‐Boltz, L. A., Kang, T., Reardon, J. T., Lee, J. H., & Öztürk, N. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.03.017 · Cited by 322
Eukaryotic nucleotide excision repair: from understanding mechanisms to influencing biology
Shuck, S. C., Short, E. A., & Turchi, J. J. (2008) · Cell Research · doi:10.1038/cr.2008.2 · Cited by 289
Systems Biology Modeling of the Radiation Sensitivity Network: A Biomarker Discovery Platform
Eschrich, S. A., Zhang, H., Zhao, H., Boulware, D. C., Lee, J., Bloom, G. C., & Torres–Roca, J. F. (2009) · International Journal of Radiation Oncology*Biology*Physics · doi:10.1016/j.ijrobp.2009.05.056 · Cited by 276
Circadian control of XPA and excision repair of cisplatin-DNA damage by cryptochrome and HERC2 ubiquitin ligase
Kang, T.-H., Lindsey-Boltz, L. A., Reardon, J. T., & Sancar, A. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0915085107 · Cited by 250
Ultraviolet radiation-induced non-melanoma skin cancer: Regulation of DNA damage repair and inflammation
Kim, I., & He, Y. (2014) · Genes & Diseases · doi:10.1016/j.gendis.2014.08.005 · Cited by 231
Solar UV damage to cellular DNA: from mechanisms to biological effects
Mullenders, L. H. F. (2018) · Photochemical & Photobiological Sciences · doi:10.1039/c8pp00182k · Cited by 225
DNA Damage and Repair: From Molecular Mechanisms to Health Implications
Fabio Altieri, F., Grillo, C., Maceroni, M., & Chichiarelli, S. (2008) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1830 · Cited by 222
SUMO under stress
Tempé, D., Piechaczyk, M., & Bossis, G. (2008) · Biochemical Society Transactions · doi:10.1042/bst0360874 · Cited by 168
RNF111/Arkadia is a SUMO-targeted ubiquitin ligase that facilitates the DNA damage response
Poulsen, S. L., Hansen, R. K., Wagner, S., van Cuijk, L., van Belle, G. J., Streicher, W. W., Wikström, M., Choudhary, C., Houtsmuller, A. B., Marteijn, J. A. F., et al. (2013) · The Journal of Cell Biology · doi:10.1083/jcb.201212075 · Cited by 175
Acquired temozolomide resistance in MGMT-deficient glioblastoma cells is associated with regulation of DNA repair by DHC2
Yi, G., Huang, G., Guo, M., Zhang, X., Wang, H., Deng, S., Li, Y., Xiang, W., Chen, Z., Pan, J., et al. (2019) · Brain · doi:10.1093/brain/awz202 · Cited by 167
Cullin 4A-mediated proteolysis of DDB2 protein at DNA damage sites regulates in vivo lesion recognition by XPC
El-Mahdy, M. A., Zhu, Q., Wang, Q.-E., Wani, G., Prætorius-Ibba, M., & Wani, A. A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m511834200 · Cited by 151
Chromatin retention of DNA damage sensors DDB2 and XPC through loss of p97 segregase causes genotoxicity
Puumalainen, M.-R., Lessel, D., Rüthemann, P., Kaczmarek, N., Bachmann, K., Ramadan, K., & Naegeli, H. (2014) · Nature Communications · doi:10.1038/ncomms4695 · Cited by 138
Evidence for Small Ubiquitin-like Modifier-dependent Nuclear Import of the Thymidylate Biosynthesis Pathway
Woeller, C. F., Anderson, D. D., Szebenyi, D. M. E., & Stover, P. J. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702526200 · Cited by 123
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
“In addition, USP7 has been suggested to indirectly influence PCNA mono-ubiqutination, by regulating the stability of the Rad18 and HLTF E3 ubiquitin ligases (Qing et al., 2011; Zlatanou et al., 2016).”
Background
SUMO and ubiquitin-dependent XPC exchange drives nucleotide excision repair
van Cuijk, L., van Belle, G. J., der Velden, Y. T.-V., Poulsen, S. L., Janssens, R. C., Theil, A. F., Sabatella, M., Lans, H., Mailand, N., Houtsmuller, A. B., et al. (2015) · Nature Communications · doi:10.1038/ncomms8499 · Cited by 113
Ubiquitin proteasome system (UPS): what can chromatin do for you?
O’Connell, B. C., & Harper, J. W. (2007) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2007.02.014 · Cited by 115
The Intertwined Roles of Transcription and Repair Proteins
Fong, Y. W., Cattoglio, C., & Tjian, R. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.10.018 · Cited by 106
DNA damage binding protein component DDB1 participates in nucleotide excision repair through DDB2 DNA-binding and cullin 4A ubiquitin ligase activity
Li, J., Wang, Q.-E., Zhu, Q., El-Mahdy, M. A., Wani, G., Prætorius-Ibba, M., & Wani, A. A. (2006) · Cancer Research · doi:10.1158/0008-5472.can-06-1115 · Cited by 106
Self-citation
Dynamic in vivo interaction of DDB2 E3 ubiquitin ligase with UV-damaged DNA is independent of damage-recognition protein XPC
Luijsterburg, M. S., Goedhart, J., Moser, J., Kool, H., Geverts, B., Houtsmuller, A. B., Mullenders, L. H. F., Vermeulen, W., & van Driel, R. (2007) · Journal of Cell Science · doi:10.1242/jcs.008367 · Cited by 105
Modulation of Nucleotide Excision Repair by Mammalian SWI/SNF Chromatin-remodeling Complex
Zhao, Q., Wang, Q.-E., Ray, A., Wani, G., Han, C., Milum, K., & Wani, A. A. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.044982 · Cited by 102
Regulation of damage recognition in mammalian global genomic nucleotide excision repair
Sugasawa, K. (2009) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2009.08.004 · Cited by 102
SUMO Interacting Motifs: Structure and Function
Yau, T. Y., Sander, W. R., Eidson, C., & Courey, A. J. (2021) · Cells · doi:10.3390/cells10112825 · Cited by 96
USP7 deubiquitinase promotes ubiquitin-dependent DNA damage signaling by stabilizing RNF168.
Zhu, Q., Sharma, N., He, J., Wani, G., & Wani, A. A. (2015) · Cell Cycle · doi:10.1080/15384101.2015.1007785 · Cited by 87
Ubiquitin-specific Protease 7 Regulates Nucleotide Excision Repair through Deubiquitinating XPC Protein and Preventing XPC Protein from Undergoing Ultraviolet Light-induced and VCP/p97 Protein-regulated Proteolysis
He, J., Zhu, Q., Wani, G., Sharma, N., Han, C., Qian, J., Pentz, K., Wang, Q., & Wani, A. A. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.589812 · Cited by 92
Novel Proteomics Strategy Brings Insight into the Prevalence of SUMO-2 Target Sites
Blomster, H. A., Hietakangas, V., Wu, J., Kouvonen, P., Hautaniemi, S., & Sistonen, L. (2009) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m800551-mcp200 · Cited by 86
Targeting Ubc9 for cancer therapy
Mo, Y.-Y., & Moschos, S. J. (2005) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.9.6.1203 · Cited by 87
Biochemical and Structural Domain Analysis of Xeroderma Pigmentosum Complementation Group C Protein
Bunick, C. G., Miller, M. R., Fuller, B. E., Fanning, E., & Chazin, W. (2006) · Biochemistry · doi:10.1021/bi061370o · Cited by 88
Regulation of Nucleotide Excision Repair by UV-DDB: Prioritization of Damage Recognition to Internucleosomal DNA
Fei, J., Kaczmarek, N., Luch, A., Glas, A. F., Carell, T., & Naegeli, H. (2011) · PLoS Biology · doi:10.1371/journal.pbio.1001183 · Cited by 88
Xeroderma pigmentosum genes: Functions inside and outside DNA repair
Sugasawa, K. (2007) · Carcinogenesis · doi:10.1093/carcin/bgm282 · Cited by 83
SUMOylation and de‐SUMOylation in response to DNA damage
Dou, H., Huang, C., Nguyen, T. V., Lu, L., & Yeh, E. T. H. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.04.002 · Cited by 88
Molecular Regulation of UV ‐Induced DNA Repair
Shah, P., & He, Y. (2015) · Photochemistry and Photobiology · doi:10.1111/php.12406 · Cited by 75
Aging Results in Differential Regulation of DNA Repair Pathways in Pachytene Spermatocytes in the Brown Norway Rat1
Paul, C., Nagano, M. C., & Robaire, B. (2011) · Biology of Reproduction · doi:10.1095/biolreprod.111.094219 · Cited by 74
Sumoylation and Regulation of Cardiac Gene Expression
Wang, J., & Schwartz, R. J. (2010) · Circulation Research · doi:10.1161/circresaha.110.220491 · Cited by 76
Gene Expression Profiles in Radiation Workers Occupationally Exposed to Ionizing Radiation
Fachin, A. L., Mello, S. S., Sandrin‐Garcia, P., Junta, C. M., Ghilardi‐Netto, T., Donadi, E. A., Passos, G. A. S., & Sakamoto‐Hojo, E. T. (2009) · Journal of Radiation Research · doi:10.1269/jrr.08034 · Cited by 78
Aberrations in DNA repair pathways in cancer and therapeutic significances
Motegi, A., Masutani, M., Yoshioka, K., & Bessho, T. (2019) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2019.02.005 · Cited by 76
A Molecular Assay of Tumor Radiosensitivity: A Roadmap Towards Biology-Based Personalized Radiation Therapy
Torres-Roca, J. F. (2012) · Personalized Medicine · doi:10.2217/pme.12.55 · Cited by 81
Histone modifications: crucial elements for damage response and chromatin restoration
Zhu, Q., & Wani, A. A. (2010) · Journal of Cellular Physiology · doi:10.1002/jcp.22060 · Cited by 72
Adaptive Posttranslational Control in Cellular Stress Response Pathways and Its Relationship to Toxicity Testing and Safety Assessment
Zhang, Q., Bhattacharya, S., Pi, J., Clewell, R. A., Carmichael, P. L., & Andersen, M. E. (2015) · Toxicological Sciences · doi:10.1093/toxsci/kfv130 · Cited by 71
Hypoxia-inducible factor-1α regulates the expression of nucleotide excision repair proteins in keratinocytes
Rezvani, H. R., Mahfouf, W., Ali, N., Chemin, C., Ged, C., Kim, A. L., de Verneuil, H., Taı̈eb, A., Bickers, D. R., & Mazurier, F. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp1072 · Cited by 73
Ubiquitin and TFIIH-stimulated DDB2 dissociation drives DNA damage handover in nucleotide excision repair
Ribeiro-Silva, C., Sabatella, M., Helfricht, A., Marteijn, J. A. F., Theil, A. F., Vermeulen, W., & Lans, H. (2020) · Nature Communications · doi:10.1038/s41467-020-18705-0 · Cited by 73
USP22 Functions as an Oncogenic Driver in Prostate Cancer by Regulating Cell Proliferation and DNA Repair
McCann, J. J., Vasilevskaya, I. A., Neupane, N. P., Shafi, A. A., McNair, C. M., Dylgjeri, E., Mandigo, A. C., Schiewer, M. J., Schrecengost, R. S., Gallagher, P., et al. (2019) · Cancer Research · doi:10.1158/0008-5472.can-19-1033 · Cited by 68
Overexpression of DDB2 enhances the sensitivity of human ovarian cancer cells to cisplatin by augmenting cellular apoptosis
Barakat, B. M., Wang, Q., Han, C., Milum, K., Yin, D., Zhao, Q., Wani, G., Arafa, E. A., El‐Mahdy, M. A., & Wani, A. A. (2009) · International Journal of Cancer · doi:10.1002/ijc.25112 · Cited by 72
Xeroderma Pigmentosum Complementation Group E Protein (XPE/DDB2): Purification of Various Complexes of XPE and Analyses of Their Damaged DNA Binding and Putative DNA Repair Properties
Kulaksiz-Erkmen, G., Reardon, J. T., & Sancar, A. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.22.9784-9792.2005 · Cited by 71
The protein shuffle
Park, C., & Choi, B. (2006) · FEBS Journal · doi:10.1111/j.1742-4658.2006.05189.x · Cited by 65
Xeroderma pigmentosum group C sensor: unprecedented recognition strategy and tight spatiotemporal regulation
Puumalainen, M.-R., Rüthemann, P., Min, J., & Naegeli, H. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-2075-z · Cited by 71
Ubiquitylation-independent degradation of Xeroderma pigmentosum group C protein is required for efficient nucleotide excision repair
Wang, Q., Prætorius-Ibba, M., Zhu, Q., Elmahdy, M., Wani, G., Zhao, Q., Qin, S., Patnaik, S., & Wani, A. A. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm550 · Cited by 67
Differential contributory roles of nucleotide excision and homologous recombination repair for enhancing cisplatin sensitivity in human ovarian cancer cells
Wang, Q., Milum, K., Han, C., Huang, Y., Wani, G., Thomale, J., & Wani, A. A. (2011) · Molecular Cancer · doi:10.1186/1476-4598-10-24 · Cited by 63
Functional regulation of the DNA damage-recognition factor DDB2 by ubiquitination and interaction with xeroderma pigmentosum group C protein
Matsumoto, S., Fischer, E. S., Yasuda, T., Dohmae, N., Iwai, S., Mori, T., Nishi, R., Yoshino, K., Sakai, W., Hanaoka, F., et al. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv038 · Cited by 59
Attenuated Expression of Xeroderma Pigmentosum Group C Is Associated with Critical Events in Human Bladder Cancer Carcinogenesis and Progression
Chen, Z., Yang, J., Gan, W., Song, B., Li, J., & Xu, Z. (2007) · Cancer Research · doi:10.1158/0008-5472.can-06-0877 · Cited by 60
The p38 Mitogen-activated Protein Kinase Augments Nucleotide Excision Repair by Mediating DDB2 Degradation and Chromatin Relaxation
Zhao, Q., Barakat, B. M., Qin, S., Ray, A., El‐Mahdy, M. A., Wani, G., Arafa, E. A., Mir, S. N., Wang, Q., & Wani, A. A. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m803963200 · Cited by 62
Such small hands: the roles of centrins/caltractins in the centriole and in genome maintenance
Dantas, T. J., Daly, O. M., & Morrison, C. G. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-0961-1 · Cited by 55
Overview of xeroderma pigmentosum proteins architecture, mutations and post-translational modifications
Feltes, B. C., & Bonatto, D. (2014) · Mutation Research/Reviews in Mutation Research · doi:10.1016/j.mrrev.2014.12.002 · Cited by 53
The Role of the COP9 Signalosome and Neddylation in DNA Damage Signaling and Repair
Chung, D., & Dellaire, G. (2015) · Biomolecules · doi:10.3390/biom5042388 · Cited by 50
LMP1-Induced Sumoylation Influences the Maintenance of Epstein-Barr Virus Latency through KAP1
Bentz, G. L., Moss, C. R., Whitehurst, C. B., Moody, C. A., & Pagano, J. S. (2015) · Journal of Virology · doi:10.1128/jvi.00711-15 · Cited by 53
SUMO-dependent regulation of centrin-2
Klein, U. R., & Nigg, E. A. (2009) · Journal of Cell Science · doi:10.1242/jcs.050245 · Cited by 51
Ubiquitin-like modifications in the DNA damage response
Wang, Z., Zhu, W., & Xu, X. (2017) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2017.07.001 · Cited by 52
Ginsenoside Rb1 Suppresses Ultraviolet Radiation-Induced Apoptosis by Inducing DNA Repair
Cai, B., Jin, S.-L., Luo, D., Xiang-fei, L., & Gao, J. (2009) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.32.837 · Cited by 47
Role of SUMO/Ubc9 in DNA Damage Repair and Tumorigenesis
Moschos, S. J., & Mo, Y.-Y. (2006) · Journal of Molecular Histology · doi:10.1007/s10735-006-9030-0 · Cited by 47
Transcriptional and Posttranslational Regulation of Nucleotide Excision Repair: The Guardian of the Genome against Ultraviolet Radiation
Park, J.-M., & Kang, T.-H. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17111840 · Cited by 44
Nucleotide excision repair leaves a mark on chromatin: DNA damage detection in nucleosomes
Apelt, K., Lans, H., Schärer, O. D., & Luijsterburg, M. S. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-03984-7 · Cited by 45
A UV-responsive Internal Ribosome Entry Site Enhances Serine Hydroxymethyltransferase 1 Expression for DNA Damage Repair
Fox, J. T., Shin, W. K., Caudill, M. A., & Stover, P. J. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.015800 · Cited by 43
The Dark Side of UV-Induced DNA Lesion Repair
Strzałka, W., Zgłobicki, P., Kowalska, E., Bażant, A., Dziga, D., & Banaś, A. K. (2020) · Genes · doi:10.3390/genes11121450 · Cited by 48
Xeroderma Pigmentosum: A Model for Human Premature Aging
Rizza, E. R. H., DiGiovanna, J. J., Khan, S. G., Tamura, D., Jeskey, J., & Kraemer, K. H. (2021) · Journal of Investigative Dermatology · doi:10.1016/j.jid.2020.11.012 · Cited by 43
Coordination of Centrosome Homeostasis and DNA Repair Is Intact in MCF-7 and Disrupted in MDA-MB 231 Breast Cancer Cells
Acu, I. D., Liu, T., Suino-Powell, K. M., Mooney, S. M., D’Assoro, A. B., Rowland, N., Muotri, A. R., Correa, R. G., Niu, Y., Kumar, R., et al. (2010) · Cancer Research · doi:10.1158/0008-5472.can-09-3800 · Cited by 42
A role for SUMO in nucleotide excision repair
Silver, H. R., Nissley, J. A., Reed, S. H., Hou, Y., & Johnson, E. S. (2011) · DNA repair · doi:10.1016/j.dnarep.2011.09.013 · Cited by 41
XPC: Going where no DNA damage sensor has gone before
Nemzow, L., Lubin, A., Zhang, L., & Gong, F. (2015) · DNA repair · doi:10.1016/j.dnarep.2015.09.004 · Cited by 45
Physical and functional interaction between DDB and XPA in nucleotide excision repair
Wakasugi, M., Kasashima, H., Fukase, Y., Imura, M., Imai, R., Yamada, S., Cleaver, J. E., & Matsunaga, T. (2008) · Nucleic Acids Research · doi:10.1093/nar/gkn964 · Cited by 40
The C-terminal Region and SUMOylation of Cockayne Syndrome Group B Protein Play Critical Roles in Transcription-coupled Nucleotide Excision Repair
Sin, Y., Tanaka, K., & Saijo, M. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.683235 · Cited by 38
SUMOylation of xeroderma pigmentosum group C protein regulates DNA damage recognition during nucleotide excision repair
Akita, M., Tak, Y.-S., Shimura, T., Matsumoto, S., Okuda-Shimizu, Y., Shimizu, Y., Nishi, R., Saitoh, H., Iwai, S., Mori, T., et al. (2015) · Scientific Reports · doi:10.1038/srep10984 · Cited by 37
Roles of Ubiquitination and SUMOylation in DNA Damage Response
Su, S., Zhang, Y., & Liu, P. (2019) · Current Issues in Molecular Biology · doi:10.21775/cimb.035.059 · Cited by 37
Transcription-coupled nucleotide excision repair is coordinated by ubiquitin and SUMO in response to ultraviolet irradiation
Liebelt, F., Schimmel, J., Vries, M. V., Klemann, E., van Royen, M. E., van der Weegen, Y., Luijsterburg, M. S., Mullenders, L. H. F., Pines, A., Vermeulen, W., et al. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz977 · Cited by 35
XPC: Its Product and Biological Roles
Sugasawa, K. (2008) · Advances in Experimental Medicine and Biology · doi:10.1007/978-0-387-09599-8_6 · Cited by 36
The ubiquitin‐proteasome system in cancer, a major player in DNA repair. Part 1: post‐translational regulation
Vlachostergios, P. J., Patrikidou, A., Daliani, D., & Papandreou, C. N. (2009) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2009.00824.x · Cited by 36
Suppressed expression of non-DSB repair genes inhibits gamma-radiation-induced cytogenetic repair and cell cycle arrest
Zhang, Y., Rohde, L. H., Emami, K., Hammond, D. K., Casey, R. C., Mehta, S. K., Jeevarajan, A. S., Pierson, D. L., & Wu, H. (2008) · DNA repair · doi:10.1016/j.dnarep.2008.07.009 · Cited by 36
Damaged DNA-binding protein down-regulates epigenetic mark H3K56Ac through histone deacetylase 1 and 2
Zhu, Q., Battu, A., Ray, A., Wani, G., Qian, J., He, J., Wang, Q., & Wani, A. A. (2015) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2015.01.005 · Cited by 34
Stimulation of DNA Glycosylase Activities by XPC Protein Complex: Roles of Protein‐Protein Interactions
Shimizu, Y., Uchimura, Y., Dohmae, N., Saitoh, H., Hanaoka, F., & Sugasawa, K. (2010) · Journal of Nucleic Acids · doi:10.4061/2010/805698 · Cited by 33
ASH1L histone methyltransferase regulates the handoff between damage recognition factors in global-genome nucleotide excision repair
Pogliano, C. B., Gatti, M., Rüthemann, P., Garajovà, Z., Penengo, L., & Naegeli, H. (2017) · Nature Communications · doi:10.1038/s41467-017-01080-8 · Cited by 34
Insight in the multilevel regulation of NER
Dijk, M., Typas, D., Mullenders, L. H. F., & Pines, A. (2014) · Experimental Cell Research · doi:10.1016/j.yexcr.2014.08.010 · Cited by 32
Inorganic arsenic inhibits the nucleotide excision repair pathway and reduces the expression of XPC
Holcomb, N., Goswami, M., Han, S. G., Scott, T., D'Orazio, J. A., Orren, D. K., Gairola, C. G., & Mellon, I. (2017) · DNA repair · doi:10.1016/j.dnarep.2017.02.009 · Cited by 33
Regulation of UV-induced DNA damage response by ubiquitylation
Bergink, S., Jaspers, N. G. J., & Vermeulen, W. (2007) · DNA repair · doi:10.1016/j.dnarep.2007.01.012 · Cited by 33
Depletion of poly(ADP-ribose) polymerase-1 reduces host cell reactivation of a UV-damaged adenovirus-encoded reporter gene in human dermal fibroblasts
Ghodgaonkar, M. M., Zacal, N., Kassam, S. N., Rainbow, A. J., & Shah, G. M. (2008) · DNA repair · doi:10.1016/j.dnarep.2008.01.001 · Cited by 30
Orchestral maneuvers at the damaged sites in nucleotide excision repair
Alekseev, S., & Coin, F. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-1859-5 · Cited by 36
XPC inhibits NSCLC cell proliferation and migration by enhancing E-Cadherin expression
Cui, T., Srivastava, A. K., Han, C., Yang, L., Zhao, R., Zou, N., Qu, M., Duan, W., Zhang, X., & Wang, Q. (2015) · Oncotarget · doi:10.18632/oncotarget.3542 · Cited by 31
The moonlighting of RAD23 in DNA repair and protein degradation
Grønbæk-Thygesen, M., Kampmeyer, C., Hofmann, K., & Hartmann‐Petersen, R. (2023) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2023.194925 · Cited by 31
Ubiquitin at work: The ubiquitous regulation of the damage recognition step of NER
van Cuijk, L., Vermeulen, W., & Marteijn, J. A. F. (2014) · Experimental Cell Research · doi:10.1016/j.yexcr.2014.07.018 · Cited by 32
The NER protein Rad33 shows functional homology to human Centrin2 and is involved in modification of Rad4
den Dulk, B., van Eijk, P., de Ruijter, M., Brandsma, J. A., & Brouwer, J. (2008) · DNA repair · doi:10.1016/j.dnarep.2008.02.004 · Cited by 30
Exposure of Human Lung Cells to Tobacco Smoke Condensate Inhibits the Nucleotide Excision Repair Pathway
Holcomb, N., Goswami, M., Han, S. G., Clark, S., Orren, D. K., Gairola, C. G., & Mellon, I. (2016) · PLoS ONE · doi:10.1371/journal.pone.0158858 · Cited by 32
Valosin-containing Protein (VCP)/p97 Segregase Mediates Proteolytic Processing of Cockayne Syndrome Group B (CSB) in Damaged Chromatin
He, J., Zhu, Q., Wani, G., Sharma, N., & Wani, A. A. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.705350 · Cited by 31
Timing of DNA lesion recognition: Ubiquitin signaling in the NER pathway
Chitale, S., & Richly, H. (2016) · Cell Cycle · doi:10.1080/15384101.2016.1261227 · Cited by 32
Nucleotide Excision Repair: Finely Tuned Molecular Orchestra of Early Pre‐incision Events
Zhu, Q., & Wani, A. A. (2016) · Photochemistry and Photobiology · doi:10.1111/php.12647 · Cited by 31
Post-translational modifications of lysine in DNA-damage repair
Chatterjee, S., Senapati, P., & Kundu, T. K. (2012) · Essays in Biochemistry · doi:10.1042/bse0520093 · Cited by 28
SUMO and the DNA damage response
Bhachoo, J. S., & Garvin, A. J. (2024) · Biochemical Society Transactions · doi:10.1042/bst20230862 · Cited by 29
Photo-Cross-Linking of XPC−Rad23B to Cisplatin-Damaged DNA Reveals Contacts with Both Strands of the DNA Duplex and Spans the DNA Adduct
Neher, T. M., Rechkunova, N. I., Lavrik, O. I., & Turchi, J. J. (2009) · Biochemistry · doi:10.1021/bi901575h · Cited by 27
Impaired repair of cyclobutane pyrimidine dimers in human keratinocytes deficient in p53 and p63
Ferguson, B. E., Li, H., Dong, T. K., Hsiao, J. L., & Oh, D. H. (2007) · Carcinogenesis · doi:10.1093/carcin/bgm244 · Cited by 28
Regulation of XPC deubiquitination by USP11 in repair of UV-induced DNA damage
Shah, P., Qiang, L., Yang, S., Soltani, K., & He, Y. (2017) · Oncotarget · doi:10.18632/oncotarget.22105 · Cited by 27

Authors: Wang, Q.-E.
Affiliations: The Ohio State University (US)
Corresponding author: Wang, Q.-E.
Venue: Nucleic Acids Research
Publisher: Oxford University Press (OUP)
Published: 2005-07-21
Volume: 33
Issue: 13
Pages: 4023-4034
ISSN: 0305-1048 (ISSN-L)
1362-4962
DOI: 10.1093/nar/gki684
PMC: PMC1178000
OpenAlex: W2154098640
Cited by: 160
References: 59
Citations by year: 2026: 2 · 2025: 2 · 2024: 2 · 2023: 6 · 2022: 2 · 2021: 9 · 2020: 6 · 2019: 7 · 2018: 2 · 2017: 8 · 2016: 9 · 2015: 13 · 2014: 11 · 2013: 3 · 2012: 7
FWCI: 4.27
Type: journal article
Language: en
Open access: gold
doi.org
Licence: other-oa
Locations: Nucleic Acids Research (publishedVersion, other-oa)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health (5r01es006074-05)
National Cancer Institute (R01CA093413, CA93413)
National Institute of Environmental Health Sciences (R01ES012991, ES12991, ES 6074)
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 › Nuclear Structure and Function
Keywords: XPC, SUMO1, ubiquitination, SUMOylation, nucleotide excision repair, UV-induced DNA damage, DDB2, XPA, ubiquitin-proteasome system, protein stabilization
MeSH terms: Cell Line, DNA-Binding Proteins, Fibroblasts, Humans, Ultraviolet Rays, Ubiquitin, SUMO-1 Protein, Proteasome Endopeptidase Complex, Xeroderma Pigmentosum Group A Protein

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

DNA repair factor XPC is modified by SUMO-1 and ubiquitin following UV irradiation.

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks