DNA repair factor XPC is modified by SUMO-1 and ubiquitin following UV irradiation.
Open accessAbstract
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.
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XPC is polyubiquitinated in response to UV-induced DNA damage by a complex containing DDB1-XPE and Cul4A E3 ubiquitin ligase.
“XPC is polyubiquitinated in cells in response to UV-induced DNA damage by a complex containing the DDB1-XPE proteins and the Cul4A E3 ubiquitin ligase (Sugasawa et al., 2005; Wang et al., 2005).”
From USP7 Is a Master Regulator of Genome Stability (2020) · cites this paper as Wang et al., 2005
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- 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
- 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
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