Usp10
- Known as:
- Usp10
- Catalog number:
- 061257A
- Product Quantity:
- 250ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- Usp10
Related genes to: Usp10
- 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
Related products to: Usp10
Related articles to: Usp10
- Cellular senescence is a complex stress response characterized not only by stable growth arrest but also by chromatin remodeling, altered proteostasis, metabolic adaptation, innate immune activation, and the senescence-associated secretory phenotype. Stress granules (SGs) are dynamic membraneless ribonucleoprotein condensates that form during translational stress and regulate mRNA triage, signaling and recovery. While both senescence and SGs represent important features of cellular stress response, the mechanisms underlying their intersection remain poorly defined. This review examines how the biology of SGs and RNA-binding proteins (RBPs) regulate senescence, with particular emphasis on stress granule-induced inflammation associated with SASP, activation of cGAS-STING, induction of NF- κB signaling, and interferon response. We discuss the differential ability of senescence inducers to generate canonical SGs and why SG formation does not necessarily result in global translational shutdown. In addition, we examine the potential roles of SG-associated RBPs, including G3BP1/2, TIA1/TIAR, CAPRIN1, USP10, HuR, ZFP36 family, FXR1, and TDP-43 together with methodological standards for identifying SGs in senescence. We present a stage-resolved modular framework describing the context-dependent functions of SG-associated RBPs throughout senescence progression and discuss therapeutic opportunities. Overall, this review suggests that stress granules and associated RNA-binding proteins should be considered context-dependent components in inflammation-driven senescence, rather than universal inducers of senescence onset. - Source: PubMed
Publication date: 2026/09/25
Bahraminasab MaryamAl-Rashdi Janan SalehDarweesh MahmoudMohammadi SaeedAl-Amri Issa SulaimanAl-Harrasi AhmedAl-Roshdi Maha Rashid - Ubiquitination is a crucial post-translational modification of proteins in eukaryotic cells. Deubiquitinating enzymes (DUBs) remove ubiquitin molecules from substrate proteins, thereby reversing ubiquitination and maintaining intracellular ubiquitin homeostasis. Dysregulation or dysfunction of DUBs is closely associated with various diseases. Among them, the ubiquitin-specific protease (USP) family, the largest subfamily of DUBs, plays a key regulatory role in tumor initiation and progression. This article systematically reviews the research progress on five representative USP family members closely linked to tumors, including USP7, USP22, USP10, USP35, and USP4, with a focus on their functional mechanisms in regulating major tumor-related signaling molecules and pathways, including p53, PTEN, c-Myc, and PD-L1. It also highlights their dual regulatory roles in tumor proliferation, resistance to apoptosis, metastasis, and immune evasion. Furthermore, this review summarizes the structural basis of USP catalysis and selectivity, the determinants of context-dependent USP functions, and the emerging roles of DUBs in tumor microenvironment remodeling and therapy resistance. We also discuss the latest advances in the development of selective inhibitors and new therapeutic modalities targeting these USPs, including PROTAC-mediated degradation, DUBTAC-mediated tumor suppressor stabilization, and molecular glue strategies. Although targeting DUBs for cancer therapy faces challenges such as substrate diversity, context-dependent functions, and functional redundancy within the family, it remains a promising strategy for tumor treatment. This review provides a theoretical foundation and research directions for further understanding the roles and mechanisms of the USP family in cancer and for developing targeted DUB-based anti-tumor therapies. - Source: PubMed
Publication date: 2026/09/10
Wang YananShi Jing - Endoplasmic reticulum stress (ERS) is a significant pathological mechanism in Parkinson's disease (PD), and prolonged ERS can ultimately lead to cellular apoptosis. This study aimed to investigate the neuroprotective effects of Lycium barbarum polysaccharides (LBP) against MPP⁺-induced damage in primary neurons. Mouse primary dopaminergic neurons were treated with MPP⁺ for 24 h to establish PD cell model, and then treated with LBP for another 24 h. Western blot analysis revealed that, compared to the Control group, MPP⁺ treatment induced primary neuron ERS and apoptosis, manifested by upregulating the expression of ERS and apoptotic marker proteins GRP78, p-IRE1α, p-eIF2α, ATF-4, CHOP, Caspase-3 and Bax, repressing mitochondrial transmembrane potential and promoting ROS production, and LBP treatment significantly counteracted MPP-induced ERS and apoptosis. Knockdown of ubiquitin-specific protease 10 (USP10) attenuated the protective effects of LBP in MPP⁺-injured primary neurons. Co-immunoprecipitation (Co-IP) and immunofluorescence co-localization assays confirmed the interaction between USP10 and Yes-associated protein 1 (YAP1). Deubiquitination experiments indicated that USP10 reduced YAP1 ubiquitination and enhanced its protein stability. Additionally, we demonstrated that USP10 suppressed the PERK/eIF2α/ATF-4/CHOP pathway, a key pro-ERS pathway, by inhibiting YAP1 ubiquitination, thereby alleviating MPP⁺-induced ERS and apoptosis. In summary, our findings indicate that LBP attenuates MPP⁺-induced neuronal injury by promoting USP10-mediated deubiquitination of YAP1 and subsequently inhibiting the PERK/eIF2α/ATF-4/CHOP signaling pathway, which proposes a new insight for the pathogenesis research of Parkinson's disease, as well as a potential pharmacological mechanism and target of Lycium barbarum polysaccharides. - Source: PubMed
Publication date: 2026/09/23
Zhang YanMa BonianZuo GuichaoJing ZhengyingDong HuiChen Guisheng - Triple-negative breast cancer (TNBC) is clinically aggressive and has few actionable molecular targets. Tubulin alpha-1B chain (TUBA1B), an alpha-tubulin isoform, has been linked to breast cancer progression, but the post-translational regulation of its abundance in TNBC remains incompletely understood. We integrated paired TNBC tissues, breast-derived cell lines, subcutaneous xenografts, an experimental lung-colonization model, immunoprecipitation-mass spectrometry, co-immunoprecipitation, colocalization, cycloheximide chase, cellular ubiquitin-associated assays, proteasome inhibition, and bidirectional genetic rescue. TUBA1B was elevated in the examined TNBC tissues and cell lines, and its manipulation altered proliferation, clonogenicity, migration-associated behavior, invasion, xenograft growth, and experimental lung colonization. USP10 was selected from the TUBA1B-associated proteome for detailed study. Endogenous co-immunoprecipitation supported an intracellular association between USP10 and TUBA1B, whereas cycloheximide chase, a cellular HA-ubiquitin-associated readout, and formal USP10-status-by-MG132 interaction analyses were consistent with USP10-associated TUBA1B stability and proteasome-sensitive turnover. Bidirectional rescue showed that TUBA1B contributes to USP10-associated cellular phenotypes. Changes in USP10 and TUBA1B were accompanied by corresponding changes in PI3K/AKT phosphorylation. These findings support a functional USP10-TUBA1B protein-stability relationship in TNBC cells that is accompanied by PI3K/AKT phosphorylation changes; direct catalytic deubiquitination and pathway causality require further testing. - Source: PubMed
Publication date: 2026/09/08
Ma HaotianXiao HuWang YiyangLi YongxiangZhao JiaweiAimaiti XiyidanHu MengjieGuo Chenming - The development of new drugs and focused treatment strategies is significantly hampered by the inadequate understanding of the complex pathophysiology of esophageal cancer (EC). Significant risk factors for the development of EC include imbalances in the oxidative stress and anti-oxidative response pathways. It has been discovered that therapeutic interventions that target the ubiquitin-specific protease 10 (USP10) and its targeted response element in response to oxidative stress can inhibit tumour growth and provide notable clinical benefits for cancer patients. To determine if USP10 is a ubiquitin-specific protease that controls oxidative stress, which in turn stabilises NOTCH1 and deactivates the anti-oxidative transcription-related pathway, and to investigate the impact of USP10 on the development of EC. As a major endogenous stabiliser of NOTCH1 intracellular domain (NICD1) function, we recognized USP10 as a protein that interacts with NICD1 and catalyses the deubiquitination of NICD1 in EC cells. Loss of USP10 specific to epithelial cells interferes with NICD1 stabilisation, which in turn stimulates the production of antioxidant genes to prevent ferroptosis caused by lipid peroxidation and significantly accelerates the development of esophageal cancer. On the other hand, in animal models treated with 4-NQO, transgenic overexpression-mediated USP10 gene therapy reduces the development of esophageal cancer. Mechanistically, USP10 binds to NICD1 in response to oxidative stress, deconjugates ubiquitination chains, and increases NICD1 abundance and the activation of its downstream signalling cascade. In vivo investigations have also shown that inhibiting USP10 expression significantly reduces the impacts that cause cancer. Importantly, a bad prognosis is indicated by reduced expression of USP10, which is linked to the severity of EC. According to these results, USP10 might be a suitable therapeutic target for the treatment of esophageal cancer. - Source: PubMed
Publication date: 2026/09/08
Tang XiufengZhang ZhiqinWei XinyiYang YanshuangShi ZongxinFan HaonanXu MinxuanLiu Chengxin