Regulation of nucleotide excision repair activity by transcriptional and post-transcriptional control of the XPA protein
Open accessAbstract
The XPA (Xeroderma pigmentosum A) protein is one of the six core factors of the human nucleotide excision repair system. In this study we show that XPA is a rate-limiting factor in all human cell lines tested, including a normal human fibroblast cell line. The level of XPA is controlled at the transcriptional level by the molecular circadian clock and at the post-translational level by a HECT domain family E3 ubiquitin ligase called HERC2. Stabilization of XPA by downregulation of HERC2 moderately enhances excision repair activity. Conversely, downregulation of XPA by siRNA reduces excision repair activity in proportion to the level of XPA. Ubiquitination and proteolysis of XPA are inhibited by DNA damage that promotes tight association of the protein with chromatin and its dissociation from the HERC2 E3 ligase. Finally, in agreement with a recent report, we find that XPA is post-translationally modified by acetylation. However, contrary to the previous claim, we find that in mouse liver only a small fraction of XPA is acetylated and that downregulation of SIRT1 deacetylase in two human cell lines does not affect the overall repair rate. Collectively, the data reveal that XPA is a limiting factor in excision repair and that its level is coordinately regulated by the circadian clock, the ubiquitin-proteasome system and DNA damage.
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The activity of NER and sensitization of cancer cells to chemotherapy can be regulated by transcriptional and post-transcriptional control of the XPA protein.
“Because of XPA’s crucial functions in NER, the activity of NER and sensitization of cancer cells to chemotherapy can be regulated by transcriptional and post-transcriptional control of the XPA protein [19], [20], [21], [22], [23], [24], [25], [26].”
From UV-Induced Nuclear Import of XPA Is Mediated by Importin-α4 in An ATR-Dependent Manner (2013) · cites this paper as [21]
XPA may serve as a potential target for sensitization to cancer chemotherapy (e.g. cisplatin) via manipulation of available nuclear XPA, either at the transcriptional or post-transcriptional level.
“XPA may serve as a potential target for sensitization to cancer chemotherapy (e.g. cisplatin) via manipulation of available nuclear XPA, either at the transcriptional or post-transcriptional level [53], [54], [55].”
From UV-Induced Nuclear Import of XPA Is Mediated by Importin-α4 in An ATR-Dependent Manner (2013) · cites this paper as [55]
XPA is part of the core NER incision complex and interacts with DNA and other NER and damage-response proteins.
“Xeroderma pigmentosum complement group A (XPA), a gene frequently mutated in XP patients, is part of the core incision complex of NER and interacts with DNA as well as many other NER and damage response proteins”
From RETRACTED: PKA-Mediated Phosphorylation of ATR Promotes Recruitment of XPA to UV-Induced DNA Damage (2014) · cites this paper as Kang et al., 2011
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- Authors
- Kang, T.-H., Reardon, J. T., & Sancar, A.
- Affiliations
- University of North Carolina at Chapel Hill (US)
- Corresponding author
- Sancar, A.
- Venue
- Nucleic Acids Research
- Publisher
- Oxford University Press (OUP)
- Published
- 2010-12-30
- Volume
- 39
- Issue
- 8
- Pages
- 3176-3187
- ISSN
- 0305-1048 (ISSN-L)
- 1362-4962
- PMC
- PMC3082913
- OpenAlex
- W2116594363
- Cited by
- 124
- References
- 45
- Citations by year
- 2026: 4 · 2025: 4 · 2024: 5 · 2023: 2 · 2022: 4 · 2021: 15 · 2020: 6 · 2019: 5 · 2018: 9 · 2017: 13 · 2016: 11 · 2015: 11 · 2014: 12 · 2013: 7 · 2012: 11
- FWCI
- 2.99
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Nucleic Acids Research (publishedVersion, cc-by-nc)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc)
- PubMed Central (publishedVersion, cc-by-nc)
- PubMed (publishedVersion)
- Carolina Digital Repository (University of North Carolina at Chapel Hill) (submittedVersion)
- UNC Libraries
- Funders
- National Institutes of Health
- National Institute of General Medical Sciences (R01GM032833, R01GM031082, GM310.82, R37GM031082, GM32833)
- National Institute of Environmental Health Sciences (P30ES010126)
- 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
- XPA, nucleotide excision repair, xeroderma pigmentosum, HERC2, E3 ubiquitin ligase, ubiquitination, protein stability, circadian clock, SIRT1, protein acetylation, DNA damage response, chromatin association, transcriptional regulation, post-transcriptional regulation, mouse liver
- MeSH terms
- Acetylation, Animals, Cell Line, DNA Damage, DNA Repair, Fibroblasts, Humans, Transcription, Genetic, Ubiquitin-Protein Ligases, Mice, Xeroderma Pigmentosum Group A Protein, Ubiquitination, Circadian Clocks
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