Ask about this productRelated genes to: USP7 antibody
- Gene:
- USP7 NIH gene
- Name:
- ubiquitin specific peptidase 7
- Previous symbol:
- HAUSP
- Synonyms:
- -
- Chromosome:
- 16p13.2
- Locus Type:
- gene with protein product
- Date approved:
- 1998-10-12
- Date modifiied:
- 2017-01-04
Related products to: USP7 antibody
Related articles to: USP7 antibody
- Following the publication of the above article, and an Expression of Concern statement (doi: 10.3892/ijo.2026.5908) that was published in light of the fact that the GAPDH control western blots shown in Fig. 5A on p. 9 were strikingly similar to the GAPDH control western blots shown in Fig. 5D, the authors have responded to the queries raised by the Editorial Office. The GAPDH panels shown in Figs. 5A and 5D were generated from the same experiment and the same set of protein lysates: Fig. 5A presented the analysis of total protein expression, whereas Fig. 5D presented immunoprecipitation analyses performed using material derived from these same experimental samples. Consequently, the GAPDH loading control was legitimately shared between the two figures. However, given that the original figure legend did not explicitly state that the same GAPDH loading control was used for both analyses, to eliminate any possible ambiguity for readers, the authors have revised Fig. 5 by replacing the representative '-MG132 panel' in Fig. 5A with results obtained from an independent repeat experiment performed under identical experimental conditions. The revised version of Fig. 5 is shown on the next page. Note that this revised figure reproduces the original findings, and does not affect the quantitative analyses, the interpretation of the data, or the conclusions of the study. Regarding a query raised by the Editorial Office concerning the presentation of flow cytometric plots in Fig. 8, the authors explained that Fig. 8E was generated by applying an additional fluorescence gate to the parent flow cytometry dataset shown in Fig. 8B, which represents standard flow cytometric analysis, rather than duplication of experimental data, and so this figure was presented correctly, and as intended by the authors. The authors thank the Editor of for granting them the opportunity to publish this corrigendum, and all the authors agree with its publication. [International Journal of Oncology 59: 89, 2021; DOI: 10.3892/ijo.2021.5269]. - Source: PubMed
Publication date: 2026/09/18
Ahmad TanveerAshraf WaseemIbrahim AbdulkhalegZaayter LiliyanaMuller Christian DHamiche AliMély YvesBronner ChristianMousli Marc - Rapid protein turnover is essential for cellular stress adaptation. HUWE1 (HECT, UBA, and WWE domain containing 1), a large HECT-type E3 ligase, regulates many short-lived stress-responsive proteins, yet the mechanisms underlying its substrate selectivity remain unclear. Here, we reveal that HUWE1 functions as a ubiquitin chain amplifier that captures pre-ubiquitinated substrates and amplifies the degradation signal by assembling long ubiquitin chains containing K11-K48 branch points, a process regulated by its partners HUWE1-associated protein stress response 1 (HAPSTR1) and USP7 (ubiquitin-specific-processing protease 7). Structural and biochemical analyses show that HAPSTR1 engages HUWE1's ubiquitin-binding motifs to drive nuclear import and modulate substrate recruitment. A cryo-EM structure of the HUWE1-USP7 complex reveals a bidirectional regulatory mechanism: HUWE1 activates USP7's catalytic activity, while USP7 modulates HUWE1 conformational states. Global proteomic analyses demonstrate that this axis drives extensive remodeling of the short-lived nuclear proteome. These findings establish the HUWE1-HAPSTR1-USP7 complex as a key ubiquitin code modifier, providing a molecular rationale for HUWE1 dysregulation in neurodevelopmental disorders and cancer. - Source: PubMed
Yatskevich StanislauMohapatra JugalMroue RanaPhu LilianLeitner AlexanderAzumaya Caleigh MVandlen RichardCheung Tommy KSoong Tik HangRose Christopher MOri AlessandroCiferri ClaudioJuszkiewicz Szymon - Hutchinson‑Gilford progeria syndrome (HGPS) is a rare premature aging disorder caused by mutations in the LMNA gene. High mobility group A1 (HMGA1) exhibits differential expression patterns across aging models. However, its roles and mechanisms in aging remain unclear. Here, we show a positive correlation between HMGA1 and the heterochromatin protein HP1β in multiple tissues of Lmna, a classic genetic mouse model of HGPS to recapitulate typical premature aging features, and naturally aging mice, and HP1β was decreased in Hmga1 mice. We further demonstrate that HMGA1 mitigates HGPS cellular senescence in a HP1β-dependent manner. Multi-omics reveals that HP1β downregulates angiopoietin-like protein 2 (ANGPTL2) by reducing chromatin accessibility, thereby suppressing SASP factors, and thus, alleviating senescence. Furthermore, HMGA1 stabilizes HP1β by recruiting de-ubiquitinating enzyme USP7. Based on the binding region of HMGA1 with HP1β and USP7, we develop a unique HMGA1 peptide (UHP) that prevents HP1β degradation, thereby ameliorating HGPS cellular senescence and significantly extending the lifespan of Lmna mice. Our findings elucidate a critical HMGA1-HP1β axis in premature aging and suggest that therapeutic strategies based on UHP may hold promise for HGPS. - Source: PubMed
Publication date: 2026/08/19
Hu QianyingSun QianXiang WeifangZhou ZilongSun HongyanHu YueYang LiehaoWang ChenyuZhang FangqingCong YujiaZhang YuXiao YichuanCong Xianling - Dysregulation of Cyclin D1 (CCND1) is implicated in various cancers, but its specific contribution to glioma radioresistance and the associated regulatory mechanisms remain largely unexplored. This research aimed to elucidate the functional role and underlying mechanisms of CCND1 in glioma radioresistance. Our findings revealed that CCND1 is significantly upregulated in glioma tissues, which correlates with a poor prognosis. Furthermore, CCND1 knockdown inhibited proliferation, triggered apoptosis, and augmented radiosensitivity in glioma cells. Additionally, CCND1 depletion sensitized glioma cells to irradiation by driving ferroptosis, as indicated by elevated reactive oxygen species (ROS) production, lipid peroxidation, and intracellular Fe accumulation. Mechanistically, USP7 was identified to stabilize the CCND1 protein via K48-linked deubiquitination. Notably, the ectopic expression of USP7 reversed the impacts of CCND1 knockdown on radiosensitivity, ferroptosis, cellular proliferation, and apoptosis. Altogether, our data indicate that the stabilization of CCND1 mediated by USP7 promotes radioresistance in glioma by suppressing ferroptosis. Therefore, targeting USP7 may serve as a promising therapeutic approach to augment the efficacy of radiotherapy in glioma. - Source: PubMed
Zhuo YayuZhang ChenruiLi XiaoyuDu ZishuoRong YirenZhang DiMi HaijuanGu XiaoyuWang FengHan HaieWu JianliangSun Jianping - The efficacy of immune checkpoint blockade in triple-negative breast cancer (TNBC) is limited by poor CD8⁺ T cell infiltration. Here, we demonstrate that tumor-derived proprotein convertase subtilisin/kexin type 9 (PCSK9) drives CD8⁺ T cell exclusion, and we identify protein arginine methyltransferase 5 (PRMT5) as an important epigenetic regulator responsible for PCSK9 expression in TNBC. Mechanistically, we elucidate that PRMT5-mediated methylation of the chromobox homolog 8 (CBX8) facilitates its interaction with the deubiquitinase USP7, which removes K33-linked ubiquitination on CBX8. This post-translational modification modulates CBX8 function, enabling it to drive the transcriptional upregulation of key downstream targets PCSK9, which inhibits CD8 T cell infiltration, and LGR5, which enhances tumor stemness. Crucially, inhibition of PRMT5 profoundly sensitizes TNBC tumors to anti-PD-1 therapy in vivo. Our work unveils a novel epigenetic pathway orchestrated by PRMT5 that converges on the functional modulation of CBX8 to synchronously governs CD8⁺ T cell exclusion and tumor stemness, nominating PRMT5 inhibition as a compelling therapeutic strategy for combination immunotherapy in TNBC. - Source: PubMed
Publication date: 2026/09/14
Chen CongcongZhang YuhengLiu ChangZhao RunkaiLiu KaimingGuo ZhiqiYang YinyinWang CongTian JiaxinGuo YanguanChen GuoJin LiyanZhu XunZhou DanyangJiang Guoqin