ReviewInternational journal of molecular sciences2026
PARylation at the Genome-Proteome Interface: Regulation of DNA Repair Protein Dynamics.
Review in International journal of molecular sciences, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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5 authors.
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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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