Selective USP7 inhibition elicits cancer cell killing through a p53-dependent mechanism.
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Ubiquitin specific peptidase 7 (USP7) is a deubiquitinating enzyme (DUB) that removes ubiquitin tags from specific protein substrates in order to alter their degradation rate and sub-cellular localization. USP7 has been proposed as a therapeutic target in several cancers because it has many reported substrates with a role in cancer progression, including FOXO4, MDM2, N-Myc, and PTEN. The multi-substrate nature of USP7, combined with the modest potency and selectivity of early generation USP7 inhibitors, has presented a challenge in defining predictors of response to USP7 and potential patient populations that would benefit most from USP7-targeted drugs. Here, we describe the structure-guided development of XL177A, which irreversibly inhibits USP7 with sub-nM potency and selectivity across the human proteome. Evaluation of the cellular effects of XL177A reveals that selective USP7 inhibition suppresses cancer cell growth predominantly through a p53-dependent mechanism: XL177A specifically upregulates p53 transcriptional targets transcriptome-wide, hotspot mutations in TP53 but not any other genes predict response to XL177A across a panel of ~500 cancer cell lines, and TP53 knockout rescues XL177A-mediated growth suppression of TP53 wild-type (WT) cells. Together, these findings suggest TP53 mutational status as a biomarker for response to USP7 inhibition. We find that Ewing sarcoma and malignant rhabdoid tumor (MRT), two pediatric cancers that are sensitive to other p53-dependent cytotoxic drugs, also display increased sensitivity to XL177A.
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USP7 inhibitors predominantly kill cancer cells by inducing p53-dependent apoptosis.
“USP7 inhibitors predominantly kill cancer cells by inducing p53-dependent apoptosis (Schauer et al., 2020).”
From USP7 Is a Master Regulator of Genome Stability (2020) · cites this paper as Schauer et al., 2020
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“USP7 inhibitors predominantly kill cancer cells by inducing p53-dependent apoptosis (Schauer et al., 2020).”
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Self-citationDiscovery of a Potent and Selective Degrader for USP7
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Self-citationHighlights in USP7 inhibitors for cancer treatment
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Targeting the deubiquitinase USP7 for degradation with PROTACs
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Targeting Ubiquitin-Specific Protease 7 (USP7) in Cancer: A New Insight to Overcome Drug Resistance
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Targeting Myc-driven stress addiction in colorectal cancer
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Regulation of Cancer Metabolism by Deubiquitinating Enzymes: The Warburg Effect
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Recent advances on the intervention sites targeting USP7-MDM2-p53 in cancer therapy
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USP7 as an emerging therapeutic target: A key regulator of protein homeostasis
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Integrating multi-omics data reveals function and therapeutic potential of deubiquitinating enzymes
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Self-citationUbiquitin-specific protease 7 (USP7): an emerging drug target for cancer treatment
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Reversal of viral and epigenetic HLA class I repression in Merkel cell carcinoma
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Self-citationProteomics-Based Identification of DUB Substrates Using Selective Inhibitors
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Self-citationIdentification and validation of selective deubiquitinase inhibitors
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Self-citationDying to Survive—The p53 Paradox
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Current and future directions of USP7 interactome in cancer study
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Deubiquitinases in hematological malignancies
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Protein post-translational modifications and tumor immunity: A pan-cancer perspective
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Indirubin-3’-monoxime acts as proteasome inhibitor: Therapeutic application in multiple myeloma
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Self-citationCovalent Small Molecule Immunomodulators Targeting the Protease Active Site
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Pro-apoptotic and anti-apoptotic regulation mediated by deubiquitinating enzymes
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Cell cycle plasticity underlies fractional resistance to palbociclib in ER+/HER2− breast tumor cells
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Ubiquitin-Specific Protease Inhibitors for Cancer Therapy: Recent Advances and Future Prospects
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DUBs Activating the Hedgehog Signaling Pathway: A Promising Therapeutic Target in Cancer
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USP7 substrates identified by proteomics analysis reveal the specificity of USP7Preprint
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Targeting MYC: Multidimensional regulation and therapeutic strategies in oncology
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Self-citationOn the Study of Deubiquitinases: Using the Right Tools for the Job
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The role of ubiquitin-specific peptidases in glioma progression
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Self-citationThe key vulnerabilities and therapeutic opportunities in the USP7-p53/MDM2 axis in cancer
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Small molecules as tools for functional assessment of deubiquitinating enzyme function
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Self-citationExtended Applications of Small-Molecule Covalent Inhibitors toward Novel Therapeutic Targets
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Diversity-oriented synthesis encoded by deoxyoligonucleotides
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Signaling pathways and targeted therapies in Ewing sarcoma
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USP7 Inhibitors Destabilize EBNA1 and Suppress Epstein‐Barr Virus Tumorigenesis
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Overcoming drug resistance by targeting protein homeostasis in multiple myeloma
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A New Insight Into p53-Inhibiting Genes in Epstein–Barr Virus-Associated Gastric Adenocarcinoma
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A review on the treatment of multiple myeloma with small molecular agents in the past five years
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Self-citationDoUBLing up: ubiquitin and ubiquitin-like proteases in genome stability
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USP7 promotes cervical cancer progression by stabilizing MTDH expression through deubiquitination
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Discovery of a Potent and Selective Degrader for USP7
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Repurposing of US-FDA-approved drugs as negative modulators of ubiquitin specific protease-7 (USP7)
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USP7 at the Crossroads of Ubiquitin Signaling, Cell Cycle, and Tumorigenesis
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Enhancing reinforcement learning for de novo molecular design applying self-attention mechanisms
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Small-molecule allosteric activator of ubiquitin-specific protease 7 (USP7)
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Self-citationAKT and DUBs: a bidirectional relationship
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Pharmacologic interrogation of USP28 cellular function in p53 signaling
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AI and machine learning in pharmaceutical formulation and manufacturing of personalized medicines
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Proteostasis of immune checkpoint receptors
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EBNA1 Upregulates P53-Inhibiting Genes in Burkitt's Lymphoma Cell Line
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Virtual screening of natural products targeting ubiquitin-specific protease 7
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The Role of Deubiquitinating Enzymes in Primary Bone Cancer
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Cellular Assays for Dynamic Quantification of Deubiquitinase Activity and Inhibition
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Renal ewing sarcoma in a young female: a case report and review of targeted therapy
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Targeting DESI2 as a Novel Therapeutic Strategy for JAK2‐Mutant Leukemias
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Role of Ubiquitin-specific Proteases in Hepatocellular Carcinoma Pathogenesis
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Discovery of N-Benzylpiperidinol derivatives as USP7 inhibitors against Hematology
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Self-citationUSP7 accelerates colorectal cancer progression by up-regulating MYO6 through deubiquitination
Jiang, M., & Xiong, C. (2025) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2025.111908 · Cited by 1 · see citing works
- Authors
- Schauer, N. J., Liu, X., Magin, R. S., Doherty, L. M., Chan, W. C., Ficarro, S. B., Hu, W., Roberts, R. M., Iacob, R. E., Stolte, B., Giacomelli, A. O., Perera, S., McKay, K., Boswell, S. A., Weisberg, E. L., Ray, A., Chauhan, D., Dhe-Paganon, S., Anderson, K. C., Griffin, J. D., Li, J., Hahn, W. C., Sorger, P. K., Engen, J. R., Stegmaier, K., Marto, J. A., & Buhrlage, S. J.
- Affiliations
- Harvard University (US)
- Brigham and Women's Hospital (US)
- Dana-Farber Cancer Institute (US)
- Northeastern University (US)
- Broad Institute (US)
- University of Vermont (US)
- Corresponding author
- Buhrlage, Sara J.
- ORCID
- Schauer, Nathan J.
- Liu, Xiaoxi
- Magin, Robert S.
- Doherty, Laura M.
- Chan, Wai Cheung
- Ficarro, Scott B.
- Hu, Wanyi
- Iacob, Roxana E.
- Giacomelli, Andrew O.
- Boswell, Sarah A.
- Weisberg, Ellen L.
- Ray, Arghya
- Chauhan, Dharminder
- Griffin, James D.
- Li, Jianing
- Hahn, William C.
- Sorger, Peter K.
- Engen, John R.
- Stegmaier, Kimberly
- Marto, Jarrod A.
- Buhrlage, Sara J.
- Venue
- Scientific Reports
- Published
- 2020-03-24
- Volume
- 10
- Issue
- 1
- Pages
- 5324-5324
- ISSN
- 2045-2322 (ISSN-L)
- PMC
- PMC7093416
- OpenAlex
- W3013382443
- Cited by
- 125
- References
- 77
- Citations by year
- 2026: 18 · 2025: 26 · 2024: 18 · 2023: 15 · 2022: 22 · 2021: 21 · 2020: 5
- FWCI
- 5.19
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Scientific Reports (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Open access LMU (Ludwid Maxmilian's Universitat Munchen) (submittedVersion, cc-by)
- Funders
- U.S. Department of Health & Human Services | National Institutes of Health
- St. Baldrick's Foundation
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
- Keywords
- USP7, p53, TP53 mutation, predictive biomarkers, structure-based drug design, tumor cell growth inhibition, Ewing sarcoma, malignant rhabdoid tumor, childhood cancer, MDM2, FOXO4, PTEN, MYCN
- MeSH terms
- Ubiquitin-Specific Peptidase 7, Antineoplastic Agents, Humans, Protease Inhibitors, Tumor Suppressor Protein p53, Apoptosis, Cell Line, Tumor, Cell Proliferation, Ubiquitination, MCF-7 Cells
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