Ask about this productRelated genes to: USP10 antibody
- Gene:
- USP10 NIH gene
- Name:
- ubiquitin specific peptidase 10
- Previous symbol:
- -
- Synonyms:
- UBPO, KIAA0190
- Chromosome:
- 16q24.1
- Locus Type:
- gene with protein product
- Date approved:
- 1999-02-01
- Date modifiied:
- 2016-01-15
- Gene:
- USP32 NIH gene
- Name:
- ubiquitin specific peptidase 32
- Previous symbol:
- -
- Synonyms:
- NY-REN-60, USP10
- Chromosome:
- 17q23.3
- Locus Type:
- gene with protein product
- Date approved:
- 2003-05-29
- Date modifiied:
- 2014-11-19
Related products to: USP10 antibody
Related articles to: USP10 antibody
- Ubiquitination is a critical post-translational modification that regulates protein stability, signalling pathways, and cellular homoeostasis. Increasing evidence shows that oncogenic viruses exploit the host ubiquitin system to promote viral persistence, immune evasion, and malignant transformation. Among the various host factors targeted, deubiquitinating enzymes (DUBs) play a pivotal role because they reverse ubiquitination, thereby regulating the stability, localization, and activity of key signalling proteins. Ubiquitin-specific peptidase 10 (USP10) has emerged as a particularly critical DUB in the context of viral tumourigenesis, functioning as a molecular rheostat that balances tumour suppression and oncogenic progression. The dysregulation of USP10 by viral oncoproteins facilitates a dual assault on the host: the subversion of innate immune sensors, specifically the RIG-I, MAVS, and cGAS-STING pathways, and the evasion of adaptive immune surveillance through the stabilisation of immune checkpoints, such as PD-L1, and the disruption of MHC-I antigen presentation. This comprehensive analysis explores the biochemical architecture of USP10, its paradoxical roles in cancer, and the specific mechanisms through which oncogenic viruses exploit this enzyme to drive malignancy and immune escape. - Source: PubMed
Li ZikeZhang DongjingChen SiqiZhang XinWang ZhihongHuang ChangshengWu QiLiu AnyiLi KangdiWei ZiranHu Junbo - Ubiquitin-specific peptidase 10 (USP10) deubiquitinates multiple signaling proteins in cancer cells. These USP10 substrates contain both tumor suppressors and oncogenic proteins, thus conferring both inhibitory and promoting effects of USP10 on tumorigenesis and progression. This review focuses on the dual roles of USP10 in various cancer types and addresses the association of aberrant USP10 expression with the development of various types of cancers, including hepatocellular carcinoma, lung cancer, breast cancer, prostate cancer, gastric cancer, and acute and chronic myelogenous leukemia. In addition, this review discusses the potential applications of USP10 inhibitors as targeted drugs for cancer therapy. - Source: PubMed
Publication date: 2026/03/13
Zhai YifeiZhou LimingZhao ManhanLin Qiong - Ubiquitination is crucial for regulating diverse cellular functions, including protein degradation, cell cycle progression, signal transduction and gene expression. This intricate process is mediated by the ubiquitin proteasome system. Within this system, ubiquitin‑specific protease 10 (USP10) is a key member that, through its deubiquitinase activity, orchestrates multiple cellular processes, such as DNA damage repair, immune and inflammatory responses, environmental adaptation and autophagy. The biological activity and protein stability of USP10 are extensively regulated by post‑translational modifications, including PARylation, histone methylation and ubiquitination. Functionally, USP10 has a dual role in tumorigenesis: It can either promote or suppress cancer progression and metastasis by influencing oncogenic signaling pathways. Beyond cancer, USP10 has been implicated in the pathogenesis of cardiovascular and neurodegenerative diseases, as well as organ fibrosis, underscoring its broad physiological relevance. Decades of research have spurred the development of a range of USP10 inhibitors, such as Spautin‑1, P22077, HBX19818, Wu‑5 and D1. The present review provides a comprehensive overview of recent advances in understanding the role of USP10 in maintaining homeostasis and dissects the pathological mechanisms in human diseases. The review further highlights the potential of precise USP10‑targeted interventions as promising therapeutic strategies for disease prevention and treatment. - Source: PubMed
Publication date: 2026/03/27
Zhang LinlinSun HuajingWang ZifanWang ZhimeiMu QiangLiu Yukun - Tumor immune escape is a major challenge in cancer treatment, and targeted immune escape therapy has become a key strategy for cancer treatment. As an important deubiquitinating enzyme, ubiquitin-specific protease 10 (USP10) participates in the process of tumor development by adjusting the balance between ubiquitination and deubiquitination of substrate proteins. Recently, USP10 has been shown to be closely related to tumor immune escape, where it serves to reduce the immunogenicity of tumor cells by stabilizing immune checkpoints and promotes tumor immune escape. In this review, we focus on the structural and functional characteristics of USP10 and elaborate on the biological function of USP10 in the occurrence and development of tumors, as well as its role in immune escape, including the regulation of immune checkpoints and the effect on immune cells in the immune microenvironment. It is possible to improve the efficacy of traditional cancer therapies by appropriately regulating the expression of USP10. The aim of this review is to provide a reference for further understanding the mechanism of tumor immune escape and the development of new tumor treatment methods. - Source: PubMed
Publication date: 2026/02/19
Huang JingjingLi NingSun JiangangLi Xiaojing - Gastric cancer (GC) continues to pose a major global health burden for which chemotherapy remains a first-line treatment. However, the efficacy of chemotherapy is often compromised by the development of chemoresistance, the underlying mechanisms of which remain elusive. Here, by profiling nascent RNA-binding proteins (nRBPs) and chromatin-binding proteins (chrBPs) in GC organoids, we identified RNA-binding motif protein 15 (RBM15) as a chromatin-associated nRBP (chr-nRBP) that is upregulated in GC cells and promotes tumour growth and chemoresistance. Mechanistically, RBM15 contains a microtubule-associated protein 1 A/1B-light chain 3 (LC3)-interacting region (LIR) motif, which is directed to the lysosome through autophagy, and impaired nucleophagy leads to its accumulation in tumours. Accumulated RBM15 recruits ubiquitin-specific peptidase 10 (USP10) to the nucleus, where it deubiquitinates and stabilizes nuclear factor erythroid 2-related factor 2 (NRF2), thereby decreasing its proteasome-mediated degradation. This RBM15-USP10-NRF2 axis drives resistance to cisplatin and 5-fluorouracil (5-FU) both in vitro and in vivo. Disruption of this pathway sensitizes GC cells to chemotherapy and suppresses tumour growth. Collectively, our findings suggest that RBM15 is both a predictive biomarker and a therapeutic target for overcoming chemotherapy resistance in GC cells. - Source: PubMed
Publication date: 2026/02/10
Ma ZhuangXu ZhengleiXu JiawenChen ChenNiu WenluWang YanjuanQian YunZhang XuYang MingStefan Sven MarcelGan LuWang ShouyuWang Bo