{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nPoly(ADP‐ribose) glycohydrolase (PARG) is the sole enzyme responsible for cleaving poly(ADP‐ribose) (PAR) chains, a modification rapidly synthesized by PARP enzymes at sites of DNA damage. By hydrolyzing PAR, PARG ensures the transient nature of this post‐translational modification, thereby promoting efficient single–strand and double–strand break repair, proper replication fork progression, and regulated cell cycle checkpoint function. Indeed, PARG has been shown to accelerate chromosomal repair processes, limit persistent PAR accumulation that would otherwise trigger cell death, and maintain genomic integrity under oxidative and genotoxic stress conditions. In addition, detailed enzymatic studies reveal that PARG possesses both exo‐ and robust endo–glycohydrolase activities that efficiently generate short, protein–free PAR chains necessary for timely restoration of normal cellular functions."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "13"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its canonical role in DNA repair, PARG influences transcriptional regulation and signaling by modulating chromatin structure and interacting with key regulatory proteins. Alternative splicing generates multiple PARG isoforms with distinct subcellular localizations—ranging from nuclear (where a short nuclear localization signal drives promoter association) to cytoplasmic and even mitochondrial pools—thus tailoring PAR turnover to the needs of various nuclear and extranuclear processes. Moreover, PARG collaborates with PARP‐1 to co–regulate global gene expression, participate in retinoic acid–dependent chromatin remodeling by controlling histone modifications, and fine–tune transforming growth factor–β/BMP–mediated signaling by regulating Smad ADP–ribosylation. In addition, post–translational modifications such as O–GlcNAcylation and interactions with proteins such as PCNA and FMRP further impact its localization and functions."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "14", "end_ref": "26"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn cancer and other disease contexts, altered PARG activity can shift the balance between cell survival and cell death. Experimental manipulation of PARG levels—through gene silencing, alternative splicing, or pharmacological inhibition—has been shown to modulate the response to DNA–damaging agents, influence replication stress, and even engender synthetic lethality in homologous recombination–deficient settings. Consistent with these findings, PARG inhibition or depletion has been linked to increased radiosensitivity in lung cancer cells, impaired metastatic behavior in colonic carcinoma, and biased outcomes in breast, pancreatic, and esophageal tumors; intriguingly, PARG functions have also been described in host–pathogen interactions that may influence infection dynamics. Such observations underscore the potential of targeting PARG, either as a single–agent strategy or in combination with chemotherapeutics, to improve outcomes in a range of oncologic and degenerative diseases."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "27", "end_ref": "36"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Anna E O Fisher, Helfrid Hochegger, Shunichi Takeda, et al. 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