ArticleScientific reports2015
SUMOylation of xeroderma pigmentosum group C protein regulates DNA damage recognition during nucleotide excision repair.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 35 citations in OpenAlex.
- Sequential post-translational modifications regulate damaged DNA-binding protein DDB2 function.Journal of biochemistry · 2024Article
- SUMO and the DNA damage response.Biochemical Society transactions · 2024Review
- Histone deacetylation regulates nucleotide excision repair through an interaction with the XPC protein.iScience · 2022Article
- Nucleotide excision repair leaves a mark on chromatin: DNA damage detection in nucleosomes.Cellular and molecular life sciences : CMLS · 2021Review
- DNA Repair in Haploid Context.International journal of molecular sciences · 2021Review
- Timely upstream events regulating nucleotide excision repair by ubiquitin-proteasome system: ubiquitin guides the way.DNA repair · 2021Review
- Chaperones for dancing on chromatin: Role of post-translational modifications in dynamic damage detection hand-offs during nucleotide excision repair.BioEssays : news and reviews in molecular, cellular and developmental biology · 2021Article
- The Molecular Basis of Ubiquitin-Conjugating Enzymes (E2s) as a Potential Target for Cancer Therapy.International journal of molecular sciences · 2021Review
- Functional impacts of the ubiquitin-proteasome system on DNA damage recognition in global genome nucleotide excision repair.Scientific reports · 2020Article
- Debulking of topoisomerase DNA-protein crosslinks (TOP-DPC) by the proteasome, non-proteasomal and non-proteolytic pathways.DNA repair · 2020Review
- Formation and Recognition of UV-Induced DNA Damage within Genome Complexity.International journal of molecular sciences · 2020Review
- A chromatin scaffold for DNA damage recognition: how histone methyltransferases prime nucleosomes for repair of ultraviolet light-induced lesions.Nucleic acids research · 2020Article
- USP22 Functions as an Oncogenic Driver in Prostate Cancer by Regulating Cell Proliferation and DNA Repair.Cancer research · 2020Article
- Molecular basis for damage recognition and verification by XPC-RAD23B and TFIIH in nucleotide excision repair.DNA repair · 2018Review
- Timing of DNA lesion recognition: Ubiquitin signaling in the NER pathway.Cell cycle (Georgetown, Tex.) · 2017Review
- Nucleotide Excision Repair: Finely Tuned Molecular Orchestra of Early Pre-incision Events.Photochemistry and photobiology · 2017Review
- Transcriptional and Posttranslational Regulation of Nucleotide Excision Repair: The Guardian of the Genome against Ultraviolet Radiation.International journal of molecular sciences · 2016Review
- Cooperativity of the SUMO and Ubiquitin Pathways in Genome Stability.Biomolecules · 2016Review
- The C-terminal Region and SUMOylation of Cockayne Syndrome Group B Protein Play Critical Roles in Transcription-coupled Nucleotide Excision Repair.The Journal of biological chemistry · 2016Article
- Lack of Associations betweenBioMed research international · 2016Article
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Authors and funding
14 authors at 6 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The xeroderma pigmentosum group C (XPC) protein complex is a key factor that detects DNA damage and initiates nucleotide excision repair (NER) in mammalian cells. Although biochemical and structural studies have elucidated the interaction of XPC with damaged DNA, the mechanism of its regulation in vivo remains to be understood in more details. Here, we show that the XPC protein undergoes modification by small ubiquitin-related modifier (SUMO) proteins and the lack of this modification compromises the repair of UV-induced DNA photolesions. In the absence of SUMOylation, XPC is normally recruited to the sites with photolesions, but then immobilized profoundly by the UV-damaged DNA-binding protein (UV-DDB) complex. Since the absence of UV-DDB alleviates the NER defect caused by impaired SUMOylation of XPC, we propose that this modification is critical for functional interactions of XPC with UV-DDB, which facilitate the efficient damage handover between the two damage recognition factors and subsequent initiation of NER.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.