Cited by 151DNA Repair MechanismsUbiquitin and proteasome pathwaysNuclear Structure and Function

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Cullin 4A-mediated Proteolysis of DDB2 Protein at DNA Damage Sites Regulates in Vivo Lesion Recognition by XPC

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El-Mahdy, Mohamed A., Zhu, Qianzheng, Wang, Qi-en, Wani, Gulzar, Prætorius-Ibba, Mette, Wani, Altaf A.·2006·Journal of Biological Chemistry

DOI 10.1074/jbc.m511834200

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Abstract

Xeroderma pigmentosum (XP) complementation group E gene product, damaged DNA-binding protein 2 (DDB2), is a subunit of the DDB heterodimeric protein complex with high specificity for binding to a variety of DNA helix-distorting lesions. DDB is believed to play a role in the initial step of damage recognition in mammalian nucleotide excision repair (NER) of ultraviolet light (UV)-induced photolesions. It has been shown that DDB2 is rapidly degraded after cellular UV irradiation. However, the relevance of DDB2 degradation to its functionality in NER is still unknown. Here, we have provided evidence that Cullin 4A (CUL-4A), a key component of CUL-4A-based ubiquitin ligase, mediates DDB2 degradation at the damage sites and regulates the recruitment of XPC and the repair of cyclobutane pyrimidine dimers. We have shown that CUL-4A can be identified in a UV-responsive protein complex containing both DDB subunits. CUL-4A was visualized in localized UV-irradiated sites together with DDB2 and XPC. Degradation of DDB2 could be blocked by silencing CUL-4A using small interference RNA or by treating cells with proteasome inhibitor MG132. This blockage resulted in prolonged retention of DDB2 at the subnuclear DNA damage foci within micropore irradiated cells. Knock down of CUL-4A also decreased recruitment of the damage recognition factor, XPC, to the damaged foci and concomitantly reduced the removal of cyclobutane pyrimidine dimers from the entire genome. These results suggest that CUL-4A mediates the proteolytic degradation of DDB2 and that this degradation event, initiated at the lesion sites, regulates damage recognition by XPC during the early steps of NER.

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Authors: El-Mahdy, M. A., Zhu, Q., Wang, Q.-E., Wani, G., Prætorius-Ibba, M., & Wani, A. A.
Affiliations: The Ohio State University (US)
The Ohio State University Comprehensive Cancer Center – Arthur G. James Cancer Hospital and Richard J. Solove Research Institute (US)
Corresponding author: Wani, Altaf A.
ORCID: Wang, Qi-en
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 2006-05
Volume: 281
Issue: 19
Pages: 13404-13411
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.m511834200
OpenAlex: W2038616578
Cited by: 151
References: 53
Citations by year: 2026: 3 · 2025: 2 · 2024: 3 · 2023: 5 · 2022: 5 · 2021: 4 · 2020: 6 · 2019: 4 · 2018: 5 · 2017: 9 · 2016: 9 · 2015: 7 · 2014: 9 · 2013: 5 · 2012: 8
FWCI: 5.43
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 5273 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Funders: National Cancer Institute (R01CA093413, CA93413)
National Institute of Environmental Health Sciences (R01ES002388, ES2388, R01ES012991, ES12991)
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: DDB2, XPC, nucleotide excision repair, DNA damage recognition, cyclobutane pyrimidine dimers, UV-induced DNA damage, ubiquitin ligase, protein degradation, DNA damage foci
MeSH terms: Cell Line, Chromatin, DNA Damage, DNA-Binding Proteins, Humans, Leupeptins, Pyrimidine Dimers, Ultraviolet Rays, Signal Transduction, Gene Silencing, Ubiquitin, Cullin Proteins

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Cullin 4A-mediated Proteolysis of DDB2 Protein at DNA Damage Sites Regulates in Vivo Lesion Recognition by XPC

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