Ubiquitin specific peptidase 7
Ubiquitin-specific peptidase 7 (USP7) is a member of the deubiquitinating enzyme family that regulates the ubiquitination state and stability of interacting proteins.
Ubiquitin-specific peptidase 7 (USP7) is a member of the deubiquitinating enzyme family that regulates the ubiquitination state and stability of interacting proteins. Its reported molecular activities include inhibition of Lys48-linked polyubiquitination, a modification commonly associated with proteasomal degradation. Accordingly, USP7 has been investigated as a regulator of proteins involved in DNA methylation, cancer-cell proliferation, metastasis, stemness, and cellular differentiation.
Recent studies position USP7 as both a mechanistic component of disease-associated signaling axes and a pharmacological target. In hepatocellular carcinoma, USP7 participates with HSP90α in stabilization of DNA methyltransferase 1 (DNMT1), linking heat stress after microwave ablation to altered DNA methylation and propionate metabolism. Other work has examined USP7 in relation to YBX1–CXCR4 signaling, CASK, the noncanonical PRC1.1 complex, and renal-fibrosis pathways involving reactive oxygen species and TGF-β1/Smad signaling. These findings extend the literature themes of cancer progression and stemness, targeted USP7 inhibition or degradation, and metabolism-associated regulation of invasion.
Rebuilt from PubMed 9 Sept 2026 · no new papers today
Where the papers sit
9 papers study ubiquitin specific peptidase 7 directly. Those 9 do not group into themes. USP7 is examined across unrelated cancers, renal fibrosis, metabolic injury, and inhibitor development. The shared focus is mechanistic and pharmacologic interrogation of USP7, without a common disease direction or consistent therapeutic trend. They are no more alike than papers drawn from anywhere in the corpus. 1 new direction follows.
USP7 is a dependency that maintains the undifferentiated state of neuroblastoma cells
In pediatric neuroblastoma treated with the USP7 inhibitor XL177A, the study found that USP7 inhibition destabilized the noncanonical PRC1.1 complex and induced a neuronal differentiation program, reducing tumor growth in cellular and animal models 41855552Mar. This assigns USP7 a role beyond the set’s usual framing as a mediator of oncogenic signaling, protein stabilization, metastasis, immune evasion, or treatment-resistant metabolism: it helps preserve a developmental cell state through PRC1.1, making forced differentiation—not only direct tumor-cell killing—the relevant therapeutic consequence.
Recent Findings on Ubiquitin specific peptidase 7
USP7 Biology and Therapeutics: USP7 stabilizes PDL1, CASK, DNMT1, and YBX1 through deubiquitination, linking it to immune evasion, malignant phenotypes, recurrence, and metastasis 42704520Sep42670798Aug42363602Jun42284889Jun. By contrast, USP7 inhibition destabilizes noncanonical PRC1.1, reduces H2AK119Ub deposition, and induces neuroblastoma differentiation 41855552Mar. In diabetic kidney disease, pirfenidone disrupts the USP7/DNMT1 complex, restores GLIS1 expression, and suppresses reactive oxygen species and TGF-β1/Smad signaling; in post-ablation hepatocellular carcinoma, USP7 contributes to DNMT1-driven DNA methylation and ACSS3 silencing 42159303May42363602Jun. Therapeutic efforts now combine USP7-directed strategies with small molecules, antibodies, methylation editing, and immunotherapy, including dauriporphine, SU056 plus SULF2 monoclonal antibody, and OAT-4828 42670798Aug42284889Jun42363602Jun42090583May. However, selective USP7 degradation produced different cellular effects from prolonged hydroxypiperidine-based inhibition, while a fluorescence polarization assay improves inhibitor evaluation and supports further structure-guided discovery 42129197May42001546Apr.
Written from 9 PubMed abstracts, each one cited by PMID above. Published: 2026-09-04. Last written: 2026-09-09 by GPT. Drafted by language models from published abstracts; not medical advice.