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
Related products to: Usp10 antibody
Related articles to: Usp10 antibody
- Pulmonary fibrosis (PF) is a lethal lung disease distinguished by deteriorating pulmonary function. This study investigated whether human umbilical cord mesenchymal stem cells (HUMSCs) alleviate PF in mice by suppressing ferroptosis through ubiquitin-specific protease 10 (USP10)-mediated deubiquitination of solute carrier family 7 member 11 (SLC7A11). - Source: PubMed
Publication date: 2026/04/29
Zhuo YiLin LanyingLin NanlongLai Fancai - Meiotic progression is critically dependent on precise regulatory networks to ensure genomic stability. SMEK1 is recognized as a regulatory subunit of the protein phosphatase 4 complex. However, its potential phosphatase-independent functions in mammalian meiosis remain largely unexplored. Given the association of genetic variants near the SMEK1 locus with human infertility, we sought to define its specific role and mechanism in murine spermatogenesis. We generated a germ cell-specific Smek1 knockout mice model by crossing Smek1 mice with Stra8-Cre mice. The phenotypic consequences were mainly assessed by histological analysis, chromosome spreading, and immunofluorescence staining. The molecular mechanisms were predominantly investigated using chromatin-immunoprecipitation, luciferase reporter assays, and co-immunoprecipitation analysis both in vivo and in vitro studies. Germ cell-specific ablation of Smek1 resulted in complete sterility due to a total arrest of spermatogenesis. The deficiency of Smek1 caused severe defects in prophase I, including an increased proportion of diplotene-stage spermatocytes, impaired synaptonemal complex dynamics, incomplete DSB repair, and a reduction in crossover. Notably, a subset of spermatocytes survived the initial checkpoint monitoring but arrested at metaphase I with a disrupted spindle structure and hyperactivation of the spindle assembly checkpoint. Mechanistically, we identified that SMEK1 functions independently of PP4 as a transcriptional repressor. It binds to the promoter of the deubiquitinating enzyme gene USP10. In the absence of SMEK1, increased USP10 protein stabilized BUBR1 (the core spindle assembly checkpoint component) and therefore delayed further progression beyond the metaphase I stage. Our study discovered a novel role for SMEK1 as a transcriptional regulator essential for meiotic progression. This SMEK1-USP10-BUBR1 pathway provides a fundamental mechanistic insight into the causes of male infertility and identifies a potential therapeutic target for human azoospermia and infertility. - Source: PubMed
Liu AiXie YunfangDuan RuonanShi HongbiaoSun PingDu YilinSun WenjieLi JiangxiaJin YechengLi XiLiu Qiji - - Source: PubMed
Publication date: 2026/04/25
Jiang YaqinWang WenjingXu HaoranPan HongLi YixuanZhao XiaofeiZhang Han - Extracellular matrix (ECM) disorder was considered as the result of fibrosis, but it is recently recognized that fibrotic ECM initiates a self-reinforcing circuit and contributes to development of fibrosis. Versican, an ECM component, participates in cell-ECM interaction and ECM regeneration. In pleura, versican is primarily derived from pleural mesothelial cells (PMCs). However, the role and mechanism of versican in pleural fibrosis remained unknown. In this study, versican and versican-mediated pleural viscoelasticity was found elevated in both human and murine pleural fibrotic tissues. Versican knockdown by shRNA prevented increases of viscoelasticity as well as pleural fibrosis. High level of versican and viscoelasticity promoted mesothelial to mesenchymal transition (MesoMT) in PMCs. Mechanistically, increased viscoelasticity induced pleural fibrosis through CD44/USP10/Smad4 mechanotransduction pathway. In conclusion, these results revealed that excessive versican in fibrotic pleural ECM enhanced ECM viscoelasticity, and consequently promoted progression of pleural fibrosis. - Source: PubMed
Publication date: 2026/04/23
Jia Zi-HengHe Xin-LiangCui Xiao-LinLi QianCheng Pei-PeiZhao Li-QinYe Shu-YiHu Shi-HeLian Chen-YueZhang He-DeLiang Li-MeiSong Lin-JieYu FanXiong LiangXiang FeiWang XiaorongWang MengDai XiyongYe HongMa Wan-Li - Osteoclast hyperactivity is a key factor in the pathogenesis of several skeletal disorders, including inflammatory bone loss, periprosthetic osteolysis, and rheumatoid arthritis. The ubiquitin-proteasome system (UPS) is pivotal in bone homeostasis and disease pathogenesis, modulating critical osteogenic and osteolytic signaling cascades. Our study identified Spautin-1, an inhibitor of ubiquitin-specific protease 10 (USP10), with the capacity to suppress osteoclastogenesis and the expression of genes associated with osteoclast activity, triggered by the nuclear factor-κB (NF-κB) ligand (RANKL) in bone marrow-derived macrophages (BMMs). Spautin-1 also effectively inhibited RANKL-induced bone resorption in vitro assays. At the molecular level, Spautin-1 reduced the expression of JNK interacting protein 1 (JIP1) by impeding USP10-mediated JIP1 deubiquitination, consequently dampening the RANKL-activated c-Jun N-terminal kinase (JNK)-mitogen-activated protein kinase (MAPK) signaling axis and curbing nuclear factor of activated T cells 1 (NFATc1) activation. Consistent with this mechanism, silencing of USP10 similarly reduced the expression of osteoclast‑related genes, mirroring the effects observed with Spautin‑1 treatment, whereas overexpression of JIP1 reversed these inhibitory effects. Additionally, Spautin-1 was found to ameliorate lipopolysaccharide (LPS)-induced bone loss in murine models. Notably, a positive correlation was observed between USP10 and JIP1 expression levels in bone tissues from osteoporotic patients. Collectively, our results position Spautin-1 as a potential therapeutic agent for osteoclast-mediated bone diseases. - Source: PubMed
Publication date: 2026/04/20
Chen XinyiXiao YueWu HanZhong MingliangZhong RongdeChen ShaoyingTang HaimeiDi QianqianZhao XibaoGao YuliChen WeiHuang QiChen Weilin