ArticleNucleic acids research2008
Loss of DNA ligase IV prevents recognition of DNA by double-strand break repair proteins XRCC4 and XLF.
Article in Nucleic acids research, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 21 citations in OpenAlex.
- O-GlcNAcylation of XRCC4 controls its stability and confers resistance to DNA double-strand break damage in cancer cells.Cell death & disease · 2026Article
- MTHFD2 is required for DNA repair and implicated in LUAD radiotherapy resistance.Journal of translational medicine · 2026Article
- The Immunogenic Role of Self-DNA in T Cell Immunity.Clinical reviews in allergy & immunology · 2025Review
- Single-molecule imaging reveals the kinetics of non-homologous end-joining in living cells.bioRxiv : the preprint server for biology · 2024Article
- XLF/Cernunnos: An important but puzzling participant in the nonhomologous end joining DNA repair pathway.DNA repair · 2017Review
- Bridging of double-stranded breaks by the nonhomologous end-joining ligation complex is modulated by DNA end chemistry.Nucleic acids research · 2017Article
- Ensemble and Single-Molecule Analysis of Non-Homologous End Joining in Frog Egg Extracts.Methods in enzymology · 2017Article
- DNA Ligase IV regulates XRCC4 nuclear localization.DNA repair · 2014Article
- E1B and E4 oncoproteins of adenovirus antagonize the effect of apoptosis inducing factor.Virology · 2014Article
- A noncatalytic function of the ligation complex during nonhomologous end joining.The Journal of cell biology · 2013Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
The repair of DNA double-strand breaks by nonhomologous end-joining (NHEJ) is essential for maintenance of genomic integrity and cell viability. Central to the molecular mechanism of NHEJ is DNA ligase IV/XRCC4/XLF complex, which rejoins the DNA. During adenovirus (Ad5) infection, ligase IV is targeted for degradation in a process that requires expression of the viral E1B 55k and E4 34k proteins while XRCC4 and XLF protein levels remain unchanged. We show that in Ad5-infected cells, loss of ligase IV is accompanied by loss of DNA binding by XRCC4. Expression of E1B 55k and E4 34k was sufficient to cause loss of ligase IV and loss of XRCC4 DNA binding. Using ligase IV mutant human cell lines, we determined that the absence of ligase IV, and not expression of viral proteins, coincided with inhibition of DNA binding by XRCC4. In ligase IV mutant human cell lines, DNA binding by XLF was also inhibited. Expression of both wild-type and adenylation-mutant ligase IV in ligase IV-deficient cells restored DNA binding by XRCC4. These data suggest that the intrinsic DNA-binding activities of XRCC4 and XLF may be subject to regulation and are down regulated in human cells that lack ligase IV.
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