Ask about this productRelated genes to: USP33 antibody
- Gene:
- USP33 NIH gene
- Name:
- ubiquitin specific peptidase 33
- Previous symbol:
- -
- Synonyms:
- KIAA1097, VDU1
- Chromosome:
- 1p31.1
- Locus Type:
- gene with protein product
- Date approved:
- 2003-09-04
- Date modifiied:
- 2016-10-05
Related products to: USP33 antibody
Related articles to: USP33 antibody
- Deubiquitination(DUB) is a critical cellular process that regulates protein stability and functionality, playing essential roles in cell proliferation, migration, tumorigenesis, and various molecular signaling pathways. Within the DUB enzyme family, ubiquitin-specific protease 33 (USP33) is found to be aberrantly expressed in several cancers, including a significant reduction in colorectal cancer (CRC) tissues. The decreased expression of USP33 impairs its ability to inhibit CRC cell proliferation, migration, and invasion, potentially through its involvement in key signaling pathways such as the β-arrestin-dependent ERK pathway, Slit-Robo pathway, and Wnt/β-catenin pathway. This review highlights the interaction between USP33 and these signaling pathways, exploring its potential as a novel independent prognostic biomarker for CRC and its promise as a therapeutic target. - Source: PubMed
Publication date: 2026/02/09
Dai YuLuo XinyuWu HengLuo YajunDeng ZijianWu JiqiangZhang LiYan Jin - This study aimed to investigate the mechanism of the involvement of USP33 in autophagic ferroptosis in endometriosis (EMs). - Source: PubMed
Publication date: 2025/12/26
Li LiYou WuZhang Mingzhe - Although gemcitabine (GEM) is the standard of care for most patients with pancreatic cancer (PC), its efficacy is limited by resistance development. Furthermore, p21-activated kinase-1 (PAK1) has been demonstrated to be involved in regulating the development of PC with GEM resistance. This study is designed to explore the role and mechanism of PAK1 in the GEM resistance of PC cells. PAK1, ubiquitin-specific peptidase 33 (USP33), methyltransferase-like 3 (METTL3), and insulin-like growth factor-2 mRNA-binding protein 3 (IGF2BP3) mRNA levels were detected using RT-qPCR. PAK1, MDR1, MRP1, USP33, METTL3, and IGF2BP3 protein levels were examined by western blot. GEM resistance, cell viability, proliferation, apoptosis, invasion, and migration were assessed using MTT, EdU, flow cytometry, transwell, and wound healing assays. After ubibrowser database analysis, the interaction between USP33 and PAK1 was verified using co-immunoprecipitation (Co-IP) assay. Meanwhile, the interaction between METTL3 and USP33 m6A was analyzed using methylated RNA immunoprecipitation (MeRIP)-qPCR and RNA immunoprecipitation (RIP) assay. A xenograft model analyzed the effects of PAK1 on GEM resistance of PC in vivo. PAK1 was upregulated in GEM-resistant PC tissues and cells. PAK1 knockdown enhanced cell sensitivity to GEM; repressed cell proliferation, invasion, and migration; and induced cell apoptosis in vitro. Mechanistically, USP33 triggered the deubiquitination of PAK1 and prevented its degradation. METTL3 stabilized USP33 mRNA through the m6A-IGF2BP3-dependent mechanism and naturally increased USP33 expression. USP33 silencing increased the drug sensitivity of PC in vivo. METTL3 supports GEM resistance of PC cells partly by regulating USP33-mediated PAK1 deubiquitination, providing a promising therapeutic target for GEM-resistant PC cells. - Source: PubMed
Publication date: 2025/10/18
He LingLi XiongbingZhen YaolanHe JiaoWang Chao - Retinoblastoma (RB) is an intraocular malignant tumor originating from primitive retinal stem cells or cone precursor cells, appearing most frequently under the age of three years. EPH receptor B2 (EPHB2) has been found to be involved in RB, but the potential action of EPHB2 in RB remains poorly understood. Real-time quantitative polymerase chain reaction and western blotting detected RNA levels and protein levels. Cell viability, proliferation, apoptosis, invasion, and stemness were evaluated by 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide, 5-ethynyl-2'deoxyuridine flow cytometry, transwell, and sphere-forming assays. The interaction between EPHB2 and ubiquitin-specific protease 33 (USP33) was confirmed by cell ubiquitination and protein stability assays. Mouse xenograft models were utilized for the validation of the effect of the USP33/EPHB2 pathway in RB. EPHB2 was upregulated in RB, and lower overall survival was observed in patients with higher levels of EPHB2. Functional experiments demonstrated that EPHB2 promoted RB cell proliferation, invasion, and stemness, as well as inhibited RB cell apoptosis in vitro. Mechanically, USP33 is responsible for EPHB2 upregulation. Additionally, USP33 caused the deubiquitination and stabilization of EPHB2 protein. Rescue experiments showed that USP33 promoted RB growth in vitro and mouse models by activating the Wnt/β-catenin signaling in an EPHB2-dependent manner. The study identified a positive regulatory role of the USP33/EPHB2 pathway in the promotion of RB malignant behaviors, suggesting that developing USP33-specific inhibitors (such as small molecule compounds) may become a new direction for RB treatment. - Source: PubMed
Publication date: 2025/08/18
Zhang JieNai ChaoWang JueSu LipingNing XiaonaGuo Chenjun - Triple-negative breast cancer (TNBC) is an aggressive malignancy lacking effective targeted therapies. Given the growing importance of regulated cell death pathways, we investigated the role of USP33 and its interaction with the tumor suppressor TAP63 in modulating ferroptosis and autophagy in TNBC. - Source: PubMed
Publication date: 2025/08/13
Qu FeilinJian WeiHuang YixiangZhou XiqianWang XuehuiLi JunJieWang GangMainly