ArticleOncogene2025
The deubiquitination-PARylation positive feedback loop of the USP10-PARP1 axis promotes DNA damage repair and affects therapeutic efficacy of PARP1 inhibitor.
Article in Oncogene, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
8 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
- MAP2K6 reprograms NADCell death & disease · 2026Article
- USP10 deubiquitinase: Physiological function, diseases and therapeutic target (Review).International journal of molecular medicine · 2026Review
- Article
- Review
- Disrupting the USP1-UAF1 deubiquitinase complex: a master regulator of replication stress and frontier target in cancer therapy.Medical oncology (Northwood, London, England) · 2026Review
- USP10 promotes cell proliferation and gemcitabine resistance in pancreatic cancer by the regulation of IGF2BP3-STEAP3.Oncogene · 2026Article
- PARylation-centric crosstalk: orchestrating immune evasion and multidrug resistance in ovarian cancer.Frontiers in immunology · 2026Review
Corrections and comments
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Authors and funding
23 authors.
Funding
Abstract
PARP1 initiates DNA repair pathways including single-strand break repair (SSBR) by recruiting multiple DNA repair factors via poly ADP-ribosylation (PARylation) of target proteins. However, how PARP1 is stabilized and activated to promote DNA damage repair remains unclear. Here we report that DNA damage generates a ROS signal, which triggers USP10 to interact with and stabilize PARP1 by deubiquitinating the K418 site in an ATM-dependent manner. In turn, PARP1 mediates PARylation of USP10 at amino acid residues D634, D645, and E648, which further promotes the deubiquitination activity of USP10 and DNA damage response to form a positive feedback loop. PARP1 is highly expressed in breast cancer tissues and positively correlates with USP10 protein levels. Moreover, breast cancer cells treated with a USP10 inhibitor show increased sensitivity to PARP1 inhibitor both in vivo and in vitro. Overall, our results unravel that the deubiquitination-PARylation positive feedback loop of the USP10-PARP1 axis promotes DNA damage repair, which might contribute to the improvement of PARP1 inhibitor efficacy in breast cancer treatment.
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Registered trials
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