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Peer-reviewedCC BYInternational journal of molecular sciences

PARylation at the Genome-Proteome Interface: Regulation of DNA Repair Protein Dynamics.

  • Su-Jin Kang1
  • Jiwon Eom2,3
  • Yubin Ko2,3
  • Soobin Yang2,3
  • Sunbok Jang2,3,4
4 affiliations
  1. 1College of Pharmacy, Dongduk Women's University, Seoul 02748, Republic of Korea.
  2. 2College of Pharmacy, Graduate School of Pharmaceutical Sciences, Ewha Womans University, Seoul 03760, Republic of Korea.
  3. 3Graduate Program in Innovative Biomaterial Convergence, Ewha Womans University, Seoul 03760, Republic of Korea.
  4. 4Graduate Program in Regulatory Science Convergence, Ewha Womans University, Seoul 03760, Republic of Korea.
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Abstract

Poly(ADP-ribosyl)ation (PARylation) is a rapid, reversible DNA damage response that promotes chromatin remodeling and the recruitment of repair factors. Genome maintenance also involves regulating the assembly, chromatin residence, exchange, and disengagement of repair proteins after lesion processing. This review examines PARylation through the lens of repair protein dynamics, distinguishing direct poly(ADP-ribose) (PAR)-dependent regulation from PAR-associated events and broader nuclear protein quality-control pathways. The strongest evidence concerns recruitment and chromatin residence. PAR binding drives XRCC1 accumulation at base excision repair (BER) and single-strand break (SSB) intermediates. In contrast, auto-PARylation promotes PARP1 release, and PARP inhibition favors persistent PARP1-DNA complexes that may require SUMO-RNF4-UFD1-p97/VCP-dependent extraction. In nucleotide excision repair (NER), PARP1-associated DDB2 regulation, ALC1 recruitment, and chromatin remodeling intersect with ubiquitin-dependent DDB2-XPC exchange. PAR-dependent condensation may add a spatial layer of protein organization, although its contribution remains context-dependent. We further discuss implications for PARP- and PARG-directed therapy and research-stage functional readouts. Together, these observations define a testable proteostatic-rheostat framework in which variable PAR signals influence the recruitment of selected repair proteins and subsequent chromatin residence; meanwhile, later extraction and turnover involve distinct, intersecting quality-control mechanisms.

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Cite

BibTeXRIS
BibTeX
@article{kang2026parylation,
  title = {{PARylation at the Genome-Proteome Interface: Regulation of DNA Repair Protein Dynamics.}},
  author = {Su-Jin Kang and Jiwon Eom and Yubin Ko and Soobin Yang and Sunbok Jang},
  journal = {International journal of molecular sciences},
  year = {2026},
  month = sep,
  doi = {10.3390/ijms27198495},
  url = {https://europepmc.org/article/MED/42883743},
  note = {CC BY},
}
RIS
TY  - JOUR
TI  - PARylation at the Genome-Proteome Interface: Regulation of DNA Repair Protein Dynamics.
AU  - Su-Jin Kang
AU  - Jiwon Eom
AU  - Yubin Ko
AU  - Soobin Yang
AU  - Sunbok Jang
PY  - 2026
DA  - 2026/09/23
JO  - International journal of molecular sciences
DO  - 10.3390/ijms27198495
UR  - https://europepmc.org/article/MED/42883743
AB  - Poly(ADP-ribosyl)ation (PARylation) is a rapid, reversible DNA damage response that promotes chromatin remodeling and the recruitment of repair factors. Genome maintenance also involves regulating the assembly, chromatin residence, exchange, and disengagement of repair proteins after lesion processing. This review examines PARylation through the lens of repair protein dynamics, distinguishing direct poly(ADP-ribose) (PAR)-dependent regulation from PAR-associated events and broader nuclear protein quality-control pathways. The strongest evidence concerns recruitment and chromatin residence. PAR binding drives XRCC1 accumulation at base excision repair (BER) and single-strand break (SSB) intermediates. In contrast, auto-PARylation promotes PARP1 release, and PARP inhibition favors persistent PARP1-DNA complexes that may require SUMO-RNF4-UFD1-p97/VCP-dependent extraction. In nucleotide excision repair (NER), PARP1-associated DDB2 regulation, ALC1 recruitment, and chromatin remodeling intersect with ubiquitin-dependent DDB2-XPC exchange. PAR-dependent condensation may add a spatial layer of protein organization, although its contribution remains context-dependent. We further discuss implications for PARP- and PARG-directed therapy and research-stage functional readouts. Together, these observations define a testable proteostatic-rheostat framework in which variable PAR signals influence the recruitment of selected repair proteins and subsequent chromatin residence; meanwhile, later extraction and turnover involve distinct, intersecting quality-control mechanisms.
SN  - 1422-0067
ER  -