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• W3109281567 abstract "Abstract PrimPol has been recently identified as a DNA damage tolerant polymerase that plays an important role in replication stress response. However, the regulatory mechanisms of PrimPol are not well defined. In this study, we identify that the deubiquitinase USP36 interferes with degradation of PrimPol to regulate the replication stress response. Mechanistically, USP36 is deubiquitinated following DNA replication stress, which in turn facilitates its upregulation and interaction with PrimPol. USP36 deubiquitinates K29-linked polyubiquitination of PrimPol and increases its protein stability. Depletion of USP36 results in replication stress-related defects and elevates cell sensitivity to DNA-damage agents, such as cisplatin and olaparib. Moreover, USP36 expression positively correlates with the level of PrimPol protein and poor prognosis in patient samples. These findings indicate that the regulation of PrimPol K29-linked ubiquitination by USP36 plays a critical role in DNA replication stress and chemotherapy response." @default.
• W3109281567 created "2020-12-07" @default.
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• W3109281567 date "2020-11-25" @default.
• W3109281567 modified "2023-10-14" @default.
• W3109281567 title "The deubiquitinase USP36 Regulates DNA replication stress and confers therapeutic resistance through PrimPol stabilization" @default.
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• W3109281567 doi "https://doi.org/10.1093/nar/gkaa1090" @default.
• W3109281567 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/7736794" @default.
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