Cited by 106DNA Repair MechanismsUbiquitin and proteasome pathwaysNuclear Structure and Function

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DNA Damage Binding Protein Component DDB1 Participates in Nucleotide Excision Repair through DDB2 DNA-binding and Cullin 4A Ubiquitin Ligase Activity

Li, Jinyou, Wang, Qi-En, Zhu, Qianzheng, El-Mahdy, Mohamed A., Wani, Gulzar, Prætorius-Ibba, Mette, Wani, Altaf A.·2006·Cancer Research

DOI 10.1158/0008-5472.can-06-1115

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Abstract

Functional defect in DNA damage binding (DDB) activity has a direct relationship to decreased nucleotide excision repair (NER) and increased susceptibility to cancer. DDB forms a complex with cullin 4A (Cul4A), which is now known to ubiquitylate DDB2, XPC, and histone H2A. However, the exact role of DDB1 in NER is unclear. In this study, we show that DDB1 knockdown in human cells impaired their ability to efficiently repair UV-induced cyclobutane pyrimidine dimers (CPD) but not 6-4 photoproducts (6-4PP). Extensive nuclear protein fractionation and chromatin association analysis revealed that upon irradiation, DDB1 protein is translocated from a loosely bound to a tightly bound in vivo chromatin fraction and the DDB1 translocation required the participation of functional DDB2 protein. DDB1 knockdown also affected the translocation of Cul4A component to the tightly bound form in UV-damaged chromatin in vivo as well as its recruitment to the locally damaged nuclear foci in situ. However, DDB1 knockdown had no effect on DNA damage binding capacity of DDB2. The data indicated that DDB2 can bind to damaged DNA in vivo as a monomer, whereas Cul4A recruitment to damage sites depends on the fully assembled complex. Our data also showed that DDB1 is required for the UV-induced DDB2 ubiquitylation and degradation. In summary, the results suggest that (a) DDB1 is critical for efficient NER of CPD; (b) DDB1 acts in bridging DDB2 and ubiquitin ligase Cul4A; and (c) DDB1 aids in recruiting the ubiquitin ligase activity to the damaged sites for successful commencement of lesion processing by NER. (Cancer Res 2006; 66(17): 8590-7)

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Authors: Li, J., Wang, Q.-E., Zhu, Q., El-Mahdy, M. A., Wani, G., Prætorius-Ibba, M., & Wani, A. A.
Affiliations: 1Radiology and Departments of
The Ohio State University (US)
ORCID: Li, Jinyou
Wang, Qi-En
Venue: Cancer Research
Publisher: American Association for Cancer Research (AACR)
Published: 2006-09-01
Volume: 66
Issue: 17
Pages: 8590-8597
ISSN: 0008-5472 (ISSN-L)
1538-7445
DOI: 10.1158/0008-5472.can-06-1115
OpenAlex: W1982085345
Cited by: 106
References: 50
Citations by year: 2026: 6 · 2025: 3 · 2024: 3 · 2023: 1 · 2022: 5 · 2021: 7 · 2020: 3 · 2019: 5 · 2018: 6 · 2017: 7 · 2016: 5 · 2015: 5 · 2014: 4 · 2013: 4 · 2012: 5
FWCI: 3.53
Type: journal article
Language: en
Open access: closed
Locations: Cancer Research (publishedVersion)
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: DDB1, DDB2, nucleotide excision repair, cyclobutane pyrimidine dimers, 6-4 photoproducts, UV-induced DNA damage, chromatin association, nuclear foci
MeSH terms: DNA Damage, DNA Repair, DNA-Binding Proteins, Fibroblasts, Gentamicins, HeLa Cells, Humans, Recombinant Proteins, Transfection, Ultraviolet Rays, Ubiquitin-Protein Ligases, Cullin Proteins

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DNA Damage Binding Protein Component DDB1 Participates in Nucleotide Excision Repair through DDB2 DNA-binding and Cullin 4A Ubiquitin Ligase Activity

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