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• W3214744515 endingPage "1607" @default.
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• W3214744515 abstract "Poly[ADP-ribose] polymerase (PARP) inhibitors can block DNA single-strand damage repair and subsequently increase double-stranded breaks (DSBs) by reducing the activity of the PARP1 protease and by preventing the PARP1 protein from dissociating from chromatin. Tumors with the BRCA mutation are particularly sensitive to PARP inhibitors. So far, PARP inhibitors (Olaparib) have been used to treat pancreatic cancer patients with BRCA mutation. However, these patients are prone to PARP inhibitor resistance. Our previous studies suggest that fructose-1,6-bisphosphatase 1 (FBP1) is responsible for the sensitivity to various anticancer agents, such as gemcitabine or mitogen-activated protein kinase kinase (MEK) inhibitors. In this study, we demonstrate that FBP1 regulates the sensitivity to PARP inhibitors in pancreatic cancer. Then, we showed that nuclear FBP1 is responsible for this process by interacting with DNA (cytosine-5)-methyltransferase 1 (DNMT1) and trapping PARP1 in chromatin. Moreover, we revealed that ubiquitin carboxyl-terminal hydrolase 7 (USP7) binds to and induces the deubiquitination of FBP1, which prevented FBP1 from translocating to the nucleus. Finally, we demonstrated that USP7 inhibitors enhanced the antitumor effect of PARP inhibitors in an FBP1-dependent manner. Collectively, our results identify a novel USP7-FBP1-DNMT1 signaling axis in pancreatic cancer, which might indicate that USP7 inhibitors and PARP inhibitors might have more powerful antitumor effects than PARP inhibitors alone in pancreatic cancer patients." @default.
• W3214744515 created "2021-12-06" @default.
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• W3214744515 date "2021-12-17" @default.
• W3214744515 modified "2023-10-16" @default.
• W3214744515 title "Deubiquitination of FBP1 by USP7 blocks FBP1–DNMT1 interaction and decreases the sensitivity of pancreatic cancer cells to PARP inhibitors" @default.
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• W3214744515 doi "https://doi.org/10.1002/1878-0261.13149" @default.
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