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14 citation(s) found for "Zhao, Fei".

Targeting MTAP increases PARP inhibitor susceptibility in triple-negative breast cancer through a feed-forward loop
Tu, Xinyi , Zhang, Yong , Hou, Jing , Zhu, Shouhai , Wu, Zheming , Hao, Yalan , Zhang, Lingxin , Weinshilboum, Richard M. , Tao, Kaixiong , Wang, Liewei , Zhu, Shouhai , Zeng, Xiangyu , Zhao, Fei , Yang, Wen‐Bin , Jiang, Qi , Weinshilboum, Richard M. , Lou, Zhenkun

Mayo Clinic

Journal of Clinical Investigation | June 30, 2025 | Volume: 135 | Issue: 13 | Pages: No page available

10.1172/jci188120 | PMID 40590219 Get It

Triple-negative breast cancer (TNBC) represents the most malignant subtype of breast cancer. The clinical application of PARP inhibitors (PARPi) is limited by the low frequency of BRCA1/2 mutations in TNBC. Here, we identified that MTAP deletion sensitized genotoxic agents in our clinical cohort of metastatic TNBC. Further study demonstrated that MTAP deficiency or inhibition rendered TNBC susceptibility to chemotherapeutic agents, particularly PARPi. Mechanistically, targeting MTAP that synergized with PARPi by disrupting the METTL16-MAT2A axis involved in methionine metabolism and depleting in vivo s-adenosylmethionine (SAM) levels. Exhausted SAM in turn impaired PARPi-induced DNA damage repair through attenuation of MRE11 recruitment and end resection by diminishing MRE11 methylation. Notably, brain metastatic TNBC markedly benefited from a lower dose of PARPi and MTAP deficiency/inhibition synergy due to the inherently limited methionine environment in the brain. Collectively, our findings revealed a feed-forward loop between methionine metabolism and DNA repair through SAM, highlighting a therapeutic strategy of PARPi combined with MTAP deficiency/inhibition for TNBC.
Mono-ubiquitination of TopBP1 by PHRF1 enhances ATR activation and genomic stability
Cai, Chenghui, Gao, Huanyao , Moon, Jaeyoung , Christyani, Grania, Hao, Yalan , Liu, Tongzheng , Lou, Zhenkun , Kim, Wootae , Lou, Zhenkun , Kim, Wootae , Zhao, Fei , Moon, Jaeyoung, Qin, Sisi

Mayo Clinic

Nucleic Acids Research | March 7, 2025 | Volume: 53 | Issue: 5 | Pages: No page available

10.1093/nar/gkaf073 | PMID 40052822 Get It

Abstract The TopBP1-ATR axis is critical for maintaining genomic stability during DNA replication stress, yet the precise regulation of TopBP1 in replication stress responses remains poorly understood. In this study, we identified PHD and Ring Finger Domains 1 (PHRF1) as an important ATR activator through its interaction with TopBP1. Our analysis revealed a correlation between PHRF1 and genomic stability in cancer patients. Mechanistically, PHRF1 is recruited to DNA lesions in a manner dependent on its PHD domain and histone methylation. Subsequently, PHRF1 mono-ubiquitinates TopBP1 at lysine 73, which enhances the TopBP1-ATR interaction and activates ATR. Depletion of PHRF1 disrupts ATR activation and sensitizes cells to replication stress-inducing agents. Furthermore, conditional knockout of Phrf1 in mice leads to early lethality and impaired ATR-Chk1 axis signaling. Collectively, our findings establish PHRF1 as a novel E3 ligase for TopBP1, coordinating the replication stress response by enhancing TopBP1-ATR signaling.
USP25 Elevates SHLD2‐Mediated DNA Double‐Strand Break Repair and Regulates Chemoresponse in Cancer
Li, Yunhui , Li, Lei , Wang, Xinshu , Yang, Yuntong , Zhou, Yujuan, Zhang, Jiyuan , Wang, Li , Jiang, Zeshan, Zhang, Tingting , Wang, Ping , Mao, Zhiyong , Liang, Shikang , Yuan, Jian , Mao, Zhiyong , Zhao, Fei , Zhang, Yuanyuan , Chen, Yuping , Wu, Chenming , Li, Lian , Zhu, Wei‐Guo , Xu, Xingzhi , Lou, Zhenkun , Yuan, Jian

Mayo Clinic

Advanced Science | May 28, 2024 | Volume: 11 | Issue: 28 | Pages: No page available

10.1002/advs.202403485 | PMID 38803048 Get It

AbstractDNA damage plays a significant role in the tumorigenesis and progression of the disease. Abnormal DNA repair affects the therapy and prognosis of cancer. In this study, it is demonstrated that the deubiquitinase USP25 promotes non‐homologous end joining (NHEJ), which in turn contributes to chemoresistance in cancer. It is shown that USP25 deubiquitinates SHLD2 at the K64 site, which enhances its binding with REV7 and promotes NHEJ. Furthermore, USP25 deficiency impairs NHEJ‐mediated DNA repair and reduces class switch recombination (CSR) in USP25‐deficient mice. USP25 is overexpressed in a subset of colon cancers. Depletion of USP25 sensitizes colon cancer cells to IR, 5‐Fu, and cisplatin. TRIM25 is also identified, an E3 ligase, as the enzyme responsible for degrading USP25. Downregulation of TRIM25 leads to an increase in USP25 levels, which in turn induces chemoresistance in colon cancer cells. Finally, a peptide that disrupts the USP25‐SHLD2 interaction is successfully identified, impairing NHEJ and increasing sensitivity to chemotherapy in PDX model. Overall, these findings reveal USP25 as a critical effector of SHLD2 in regulating the NHEJ repair pathway and suggest its potential as a therapeutic target for cancer therapy.
Targeting MTAP creates a therapeutic vulnerability to PARP inhibition in brain metastatic TNBC by disrupting MAT2A mediated methionine metabolism
Lou, Zhenkun , Zhao, Fei , Zhang, Lingxin , Weinshilboum, Richard M. , Tao, Kaixiong , Lou, Zhenkun , Zeng, Xiangyu , Zhang, Lingxin, Weinshilboum, Richard M.

Mayo Clinic

No container title available | November 20, 2023 | Volume: No volume available | Issue: No issue available | Pages: No page available

10.21203/rs.3.rs-3579438/v1 Get It

Abstract Triple-negative breast cancer (TNBC) is an aggressive form of breast cancer with limited therapeutic strategy and unfavorable prognosis, especially for patients bearing brain metastasis. Here, we demonstrate that MTAP gene deletion or MTAP inhibition by MTAP inhibitor, MTDIA, sensitizes breast cancer cells to poly (ADP-ribose) polymerase (PARP) inhibitor (PARPi). Mechanistically, PARPi suppresses the expression of methionine adenosyltransferase 2A (MAT2A) by inducing METTL16 auto-inhibition mediated intron retention. Given that MAT2A and MTAP are key enzymes in methionine metabolism, the dual inhibition of MAT2A and MTAP disrupts methionine metabolism and leads to reduced s-adenosylmethionine. Dietary methionine restriction further boosts the combined anti-tumor efficacy of MTAP depletion/inhibition and PARPi. Most importantly, in brain metastatic TNBC, due to the natural low methionine environment in the brain, the combination of MTAP depletion/inhibition and PARPi confers significant therapeutic efficacy. Therefore, our findings provide a promising strategy for inhibiting primary or brain metastatic TNBC.
Targeting BCL6 in Gastrointestinal Stromal Tumor Promotes p53-Mediated Apoptosis to Enhance the Antitumor Activity of Imatinib
Zhao, Fei , Jia, Jie , Ma, Xianxiong , Jiang, Qi , Zhang, Ruizhi , Li, Chengguo , Wang, Tao , Liu, Weizhen , Hao, Yalan , Tao, Kaixiong , Zhang, Peng , Zeng, Xiangyu , Zhao, Fei , Jia, Jie , Ma, Xianxiong , Jiang, Qi , Zhang, Ruizhi , Li, Chengguo , Wang, Tao , Liu, Weizhen , Hao, Yalan , Tao, Kaixiong , Lou, Zhenkun , Zhang, Peng , Zeng, Xiangyu , Lou, Zhenkun

Mayo Clinic

Cancer Research | August 9, 2023 | Volume: 83 | Issue: 21 | Pages: 3624-3635

10.1158/0008-5472.can-23-0082 | PMID 37556508 Get It

Abstract Imatinib mesylate (IM) has revolutionized the treatment of gastrointestinal stromal tumor (GIST). However, most patients inevitably acquire IM resistance. Second- and third-line treatments exhibit modest clinical benefits with a median time to disease progression of 4 to 6 months, highlighting the urgency for novel therapeutic approaches. Here, we report that the expression of BCL6, a known oncogenic driver and transcriptional repressor, was significantly induced in GIST cells following IM treatment. Elevated BCL6 levels suppressed apoptosis and contributed to IM resistance. Mechanistically, BCL6 recruited SIRT1 to the TP53 promoter to modulate histone acetylation and transcriptionally repress TP53 expression. The reduction in p53 subsequently attenuated cell apoptosis and promoted tolerance of GIST cells to IM. Concordantly, treatment of GIST cells showing high BCL6 expression with a BCL6 inhibitor, BI-3802, conferred IM sensitivity. Furthermore, BI-3802 showed striking synergy with IM in IM-responsive and IM-resistant GIST cells in vitro and in vivo. Thus, these findings reveal a role for BCL6 in IM resistance and suggest that a combination of BCL6 inhibitors and IM could be a potentially effective treatment for GIST. Significance: BCL6 drives resistance to imatinib by inhibiting p53-mediated apoptosis and can be targeted in combination with imatinib to synergistically suppress tumor growth, providing a therapeutic strategy for treating gastrointestinal stromal tumor.
Syk-dependent alternative homologous recombination activation promotes cancer resistance to DNA targeted therapy
Zhou, Qin , Tu, Xinyi , Hou, Xiaonan , Yu, Jia, Zhao, Fei , Huang, Jinzhou , Olson, Anna, Gao, Ming , Luo, Kuntian, Schoolmeester, Kenneth, Weroha, S. John , Wang, Liewei , Mutter, Robert W. , Kloeber, Jake, Zhu, Shouhai , Wu, Zheming , Zeng, Xiangyu , Weroha, John, Mutter, Robert, Lou, Zhenkun , Yu, Jia, Kloeber, Jake A. , Zhang, Yong , Sun, Chenyu , Lou, Zhenkun

Mayo Clinic

No container title available | June 9, 2023 | Volume: No volume available | Issue: No issue available | Pages: No page available

10.21203/rs.3.rs-2922520/v1 | PMID 37333340 Get It

Abstract Enhanced DNA repair is an important mechanism of inherent and acquired resistance to DNA targeted therapies, including poly ADP ribose polymerase inhibition. Spleen associated tyrosine kinase (Syk) is a non-receptor tyrosine kinase known to regulate immune cell function, cell adhesion, and vascular development. Here, we report that Syk can be expressed in high grade serous ovarian cancer and triple negative breast cancers and promotes DNA double strand break resection, homologous recombination (HR) and therapeutic resistance. We found that Syk is activated by ATM following DNA damage and is recruited to DNA double strand breaks by NBS1. Once at the break site, Syk phosphorylates CtIP, a key mediator of resection and HR, at Thr-847 to promote repair activity, specifically in Syk expressing cancer cells. Syk inhibition or genetic deletion abolished CtIP Thr-847 phosphorylation and overcame the resistant phenotype. Collectively, our findings suggest that Syk drives therapeutic resistance by promoting DNA resection and HR through a novel ATM-Syk-CtIP pathway, and that Syk is a new tumor-specific target to sensitize Syk-expressing tumors to PARPi and other DNA targeted therapy.
USP37 regulates DNA damage response through stabilizing and deubiquitinating BLM
Wu, Chenming , Chen, Junliang , Su, Yang , Li, Lei , Chen, Yuping , Li, Yunhui , Wu, Jinhuan , Huang, Jinzhou , Wang, Wenrui , Yin, Hui , Jin, Mingpeng , Zhu, Wei‐Guo , Luo, Kuntian, Lou, Zhenkun , Yuan, Jian , Chang, Yiming, Zhao, Fei , Wang, Shunli , Lou, Zhenkun , Zhang, Jie , Yuan, Jian

Mayo Clinic

Nucleic Acids Research | September 10, 2021 | Volume: 49 | Issue: 19 | Pages: 11224-11240

10.1093/nar/gkab842 | PMID 34606619 Get It

Abstract The human RecQ helicase BLM is involved in the DNA damage response, DNA metabolism, and genetic stability. Loss of function mutations in BLM cause the genetic instability/cancer predisposition syndrome Bloom syndrome. However, the molecular mechanism underlying the regulation of BLM in cancers remains largely elusive. Here, we demonstrate that the deubiquitinating enzyme USP37 interacts with BLM and that USP37 deubiquitinates and stabilizes BLM, thereby sustaining the DNA damage response (DDR). Mechanistically, DNA double-strand breaks (DSB) promotes ATM phosphorylation of USP37 and enhances the binding between USP37 and BLM. Moreover, knockdown of USP37 increases BLM polyubiquitination, accelerates its proteolysis, and impairs its function in DNA damage response. This leads to enhanced DNA damage and sensitizes breast cancer cells to DNA-damaging agents in both cell culture and in vivo mouse models. Collectively, our results establish a novel molecular mechanism for the USP37–BLM axis in regulating DSB repair with an important role in chemotherapy and radiotherapy response in human cancers.
Elevated METTL16 expression in PDAC confers synthetic lethality to PARP inhibition by antagonizing MRE11-mediated DNA end resection
Kloeber, Jake A. , Mer, Georges , Lou, Zhenkun , Lou, Zhenkun , Kloeber, Jake A , Zeng, Xiangyu , Zhao, Fei , Deshpande, Rajashree A. , Paull, Tanya T.

Mayo Clinic

No container title available | June 25, 2021 | Volume: No volume available | Issue: No issue available | Pages: No page available

10.21203/rs.3.rs-598847/v1 Get It

Abstract Pancreatic ductal adenocarcinoma (PDAC) is one of the most lethal cancers worldwide. Characterization of the recurrent genetic alterations in PDAC will yield improved understanding and therapies for this disease. Here, we report that PDAC patients with elevated expression of METTL16, one of the “writers” of RNA N6-methyladenosine (m6A) modification, may benefits from poly (ADP-ribose) polymerase (PARP) inhibitor treatment. Mechanistically, METTL16 interacts with MRE11 in an RNA-dependent manner; and, this interaction inhibits MRE11’s exonuclease activity in a methyltransferase-independent manner, thereby repressing DNA end resection. Upon DNA damage, ATM phosphorylates METTL16 at Ser419 within its C terminus, resulting in METTL16 conformational change and autoinhibition of its RNA binding. This dissociates the METTL16-RNA-MRE11 complex and releases inhibition of MRE11. Concordantly, PDAC cells with high METTL16 expression levels show increased sensitivity to PARP inhibitors, especially when combined with gemcitabine. Thus, our findings have revealed a role for METTL16 in homologous recombination repair and suggest that combination of PARP inhibitors with gemcitabine could be an effective treatment strategy for PDAC patients with high METTL16 expression.
MET Amplification Attenuates Lung Tumor Response to Immunotherapy by Inhibiting STING
Yang, Qifan, Zeng, Xiangyu , Wang, Manxiang , Tu, Xinyi , Wei, Ting , Xie, Wenzhuan , Guo, Qiang , Kloeber, Jake A. , Cao, Yueyu, Guo, Guijie , Zhou, Qin , Huang, Jinzhou , Zhang, Kai , Luo, Kuntian, Kim, Wootae , Hou, Jing , Shi, Yu , Zhu, Qian , Hu, Sheng , Yue, Junqiu , Pi, Guoliang , Kloeber, Jake A , Liu, Li , Kim, Wootae , Zhu, Qian , Wei, Ting , Zeng, Xiangyu , Zhang, Yong , Dong, Shuang , Yang, Bin , Zhang, Chao , Zhao, Fei Linda , Liu, Li , Wang, Mingwei , Yin, Ping , Deng, Min , Chen, Lifeng , Lou, Zhenkun , Guo, Guijie

Mayo Clinic

Cancer Discovery | June 7, 2021 | Volume: 11 | Issue: 11 | Pages: 2726-2737

10.1158/2159-8290.cd-20-1500 | PMID 34099454 Get It

Abstract Immune checkpoint blockade (ICB) has revolutionized cancer therapy. However, the response of patients to ICB is difficult to predict. Here, we examined 81 patients with lung cancer under ICB treatment and found that patients with MET amplification were resistant to ICB and had a poor progression-free survival. Tumors with MET amplifications had significantly decreased STING levels and antitumor T-cell infiltration. Furthermore, we performed deep single-cell RNA sequencing on more than 20,000 single immune cells and identified an immunosuppressive signature with increased subsets of XIST- and CD96-positive exhausted natural killer (NK) cells and decreased CD8+ T-cell and NK-cell populations in patients with MET amplification. Mechanistically, we found that oncogenic MET signaling induces phosphorylation of UPF1 and downregulates tumor cell STING expression via modulation of the 3′-UTR length of STING by UPF1. Decreased efficiency of ICB by MET amplification can be overcome by inhibiting MET. Significance: We suggest that the combination of MET inhibitor together with ICB will overcome ICB resistance induced by MET amplification. Our report reveals much-needed information that will benefit the treatment of patients with primary MET amplification or EGFR–tyrosine kinase inhibitor resistant-related MET amplification. This article is highlighted in the In This Issue feature, p. 2659
DOCK7 protects against replication stress by promoting RPA stability on chromatin
Gao, Ming , Guo, Guijie , Huang, Jinzhou , Hou, Xiaonan , Ham, Hyoungjun , Kim, Wootae , Tu, Xinyi , Zhou, Qin , Zhang, Chao , Zhu, Qian , Liu, Jiaqi , Xu, Zhijie , Luo, Kuntian, Weroha, S. John , Billadeau, Daniel D. , Yan, Yuanliang, Weroha, John, Kim, Wootae , Xu, Zhijie , Zhao, Fei , Yan, Yuanliang , Yin, Ping , Deng, Min , Lou, Zhenkun , Guo, Guijie

Mayo Clinic

Nucleic Acids Research | March 2, 2021 | Volume: 49 | Issue: 6 | Pages: 3322-3337

10.1093/nar/gkab134 | PMID 33704464 Get It

Abstract RPA is a critical factor for DNA replication and replication stress response. Surprisingly, we found that chromatin RPA stability is tightly regulated. We report that the GDP/GTP exchange factor DOCK7 acts as a critical replication stress regulator to promote RPA stability on chromatin. DOCK7 is phosphorylated by ATR and then recruited by MDC1 to the chromatin and replication fork during replication stress. DOCK7-mediated Rac1/Cdc42 activation leads to the activation of PAK1, which subsequently phosphorylates RPA1 at S135 and T180 to stabilize chromatin-loaded RPA1 and ensure proper replication stress response. Moreover, DOCK7 is overexpressed in ovarian cancer and depleting DOCK7 sensitizes cancer cells to camptothecin. Taken together, our results highlight a novel role for DOCK7 in regulation of the replication stress response and highlight potential therapeutic targets to overcome chemoresistance in cancer.