ArticleNucleic acids research2016
Femtosecond near-infrared laser microirradiation reveals a crucial role for PARP signaling on factor assemblies at DNA damage sites.
Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 29 citations in OpenAlex.
- Liquid‒liquid phase separation and poly(ADP‒ribosyl)ation in the context of ultraviolet radiation-induced stress in mammalian cells.Biophysical reviews · 2025Review
- Dissection of DNA damage and repair pathways in live cells by femtosecond laser microirradiation and free-electron modeling.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Laser microirradiation as a tool to investigate the role of liquid-liquid phase separation in DNA damage repair.STAR protocols · 2022Article
- PARP Inhibitor Olaparib Causes No Potentiation of the Bleomycin Effect in VERO Cells, Even in the Presence of Pooled ATM, DNA-PK, and LigIV Inhibitors.International journal of molecular sciences · 2020Article
- Nuclear Accumulation of LAP1:TRF2 Complex during DNA Damage Response Uncovers a Novel Role for LAP1.Cells · 2020Article
- Article
- Laser Scissors and Tweezers to Study Chromosomes: A Review.Frontiers in bioengineering and biotechnology · 2020Review
- Genetic Material Manipulation and Modification by Optical Trapping and Nanosurgery-A Perspective.Frontiers in bioengineering and biotechnology · 2020Review
- NAD+ consumption by PARP1 in response to DNA damage triggers metabolic shift critical for damaged cell survival.Molecular biology of the cell · 2019Article
- Biphasic recruitment of TRF2 to DNA damage sites promotes non-sister chromatid homologous recombination repair.Journal of cell science · 2018Article
- Laser Microirradiation to Study In Vivo Cellular Responses to Simple and Complex DNA Damage.Journal of visualized experiments : JoVE · 2018Article
- Article
- Simultaneous dual-channel imaging to quantify interdependent protein recruitment to laser-induced DNA damage sites.Nucleus (Austin, Tex.) · 2018Article
- SIRT6 interacts with TRF2 and promotes its degradation in response to DNA damage.Nucleic acids research · 2017Article
- Low-level infrared laser modulates muscle repair and chromosome stabilization genes in myoblasts.Lasers in medical science · 2016Article
- Laser Nano-Neurosurgery from Gentle Manipulation to Nano-Incision of Neuronal Cells and Scaffolds: An Advanced Neurotechnology Tool.Frontiers in neuroscience · 2016Review
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Laser microirradiation is a powerful tool for real-time single-cell analysis of the DNA damage response (DDR). It is often found, however, that factor recruitment or modification profiles vary depending on the laser system employed. This is likely due to an incomplete understanding of how laser conditions/dosages affect the amounts and types of damage and the DDR. We compared different irradiation conditions using a femtosecond near-infrared laser and found distinct damage site recruitment thresholds for 53BP1 and TRF2 correlating with the dose-dependent increase of strand breaks and damage complexity. Low input-power microirradiation that induces relatively simple strand breaks led to robust recruitment of 53BP1 but not TRF2. In contrast, increased strand breaks with complex damage including crosslinking and base damage generated by high input-power microirradiation resulted in TRF2 recruitment to damage sites with no 53BP1 clustering. We found that poly(ADP-ribose) polymerase (PARP) activation distinguishes between the two damage states and that PARP activation is essential for rapid TRF2 recruitment while suppressing 53BP1 accumulation at damage sites. Thus, our results reveal that careful titration of laser irradiation conditions allows induction of varying amounts and complexities of DNA damage that are gauged by differential PARP activation regulating protein assembly at the damage site.
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