ArticleFASEB journal : official publication of the Federation of American Societies for Experimental Biology2025
Poly (ADP-Ribose) Glycohydrolase-Dependent dePARylation of PCNA Is Essential for DNA Replication.
Article in FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- SOCS3 Stabilizes PARP1 to Suppress Adipogenic Transcription and Abdominal Adipogenesis in Avian.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026Article
- The Expanding Landscape of ADP-Ribosylation: Protein, DNA, RNA, and Mitochondrial Regulation.Chemical research in toxicology · 2026Review
- Targeting MARylation and DePARylation in Cancer Therapy: New Promising Therapeutic Opportunities.Cancers · 2025Review
- Poly (ADP-Ribose) Glycohydrolase-Dependent dePARylation of PCNA Is Essential for DNA Replication.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025Article
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Authors and funding
12 authors.
Funding
Abstract
Poly (ADP-ribosyl)ation (PARylation) plays a crucial role in DNA replication, particularly during S phase, where it is detected at replication sites on the lagging strand to facilitate Okazaki fragment processing. However, the role of dePARylation in DNA replication remains elusive. In this study, we demonstrate that poly (ADP-ribose) glycohydrolase (PARG) is actively involved in degrading poly (ADP-ribose) at DNA replication sites during S phase. Inhibition of PARG in S-phase cells leads to the accumulation of DNA single-strand breaks at replication sites. Furthermore, suppression of dePARylation during S phase impairs DNA replication, which can be rescued by wild-type PARG but not by a catalytically inactive PARG mutant. Mechanistically, we show that PCNA, a key factor in DNA replication, is PARylated by PARP1 during S phase, which reduces its interaction with FEN1. Timely removal of PARylation from PCNA by PARG restores the interaction between PCNA and FEN1, thereby facilitating DNA replication. Taken together, our findings reveal that PARG promotes DNA replication through the dePARylation of PCNA during S phase, highlighting the critical role of PARG in DNA replication.
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