STUB1 Antibody
- Known as:
- STUB1 Antibody
- Catalog number:
- 32199
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Signalway
- Gene target:
- STUB1 Antibody
Related genes to: STUB1 Antibody
- Gene:
- STUB1 NIH gene
- Name:
- STIP1 homology and U-box containing protein 1
- Previous symbol:
- -
- Synonyms:
- UBOX1, CHIP, SDCCAG7, HSPABP2, NY-CO-7
- Chromosome:
- 16p13.3
- Locus Type:
- gene with protein product
- Date approved:
- 1999-11-25
- Date modifiied:
- 2017-12-06
Related products to: STUB1 Antibody
Related articles to: STUB1 Antibody
- Adenine deaminase (ADAR) is a key RNA editing enzyme that plays an important role in the initiation and progression of cancer. However, the mechanisms regulating its protein stability and its function in glioblastoma (GBM) remain unclear. - Source: PubMed
Publication date: 2026/08/06
Fei QinHuang JueruZhang YufengHe YiFu Qiang - Doxorubicin (DOX) is a potent anti-tumor drug that is commonly associated with cardiotoxic reactions (DIC) during its use. Ferroptosis in cardiomyocytes is one of the key pathogenic mechanisms of this toxic reaction. Forsythiaside B (FTB) has been proven to have cardioprotective effects, but its role and potential mechanism in DIC remain unknown. - Source: PubMed
Publication date: 2026/08/20
Hu SailingLv LingchunHuang Zhouqing - Aberrant tumor metabolism plays a crucial role in establishing and sustaining an immunosuppressive microenvironment. CD73, a key enzyme in the purine metabolism pathway, is frequently overexpressed in tumors, leading to elevated extracellular adenosine (ADO) levels. This accumulation suppresses antitumor immune responses by promoting immune cell exhaustion, ultimately contributing to immunotherapy resistance. However, the mechanisms underlying CD73 upregulation in tumors remain poorly defined. Here, we identify aurora kinase B (AURKB) as a critical regulator of CD73 overexpression in renal cell carcinoma (RCC), orchestrating immune evasion and resistance to immune checkpoint therapy. AURKB is highly expressed in RCC, with its prognostic significance being especially evident in tumors with strong immunogenicity. Mechanistically, AURKB enhances CD73 expression, thereby promoting T cell dysfunction and immune suppression. Mass cytometry (CyTOF) analysis revealed that AURKB inhibition facilitates immune infiltration and alleviates immune exhaustion. We further demonstrate that AURKB directly interacts with CD73 and phosphorylates it at serine 429, which inhibits STUB1-mediated ubiquitination and proteasomal degradation of CD73. Targeting AURKB to modulate the post-translational stability of CD73 restores antitumor immunity and synergizes with immune checkpoint blockade in vivo. Collectively, this study uncovers a previously unrecognized AURKB-CD73 axis and provides a mechanistically informed strategy to enhance immunotherapy efficacy in RCC. - Source: PubMed
Publication date: 2026/08/18
Tang TianyuYang WupingLu MinghaoPeng DingLi ShiqiCui SijiaYe SunyiLiu JiandongWang YifanWu CunjinTeng HaoyangHuang HaojieXu XinXia DanZhu Yi - - Source: PubMed
Publication date: 2026/08/17
Che HongZhao BingjieYi WenjingLiu PeijiaHu Lian - Pancreatic ductal adenocarcinoma (PDAC) exhibits profound metabolic plasticity that underlies its aggressive growth and therapeutic resistance. However, genetic determinants that modulate PDAC sensitivity to glycolytic inhibition remain incompletely defined. Here, we performed a pooled genome-wide CRISPR-Cas9 dropout screen in PDAC cells under 2-deoxy-D-glucose (2-DG) selection and identified FGD5 as a key regulator of glycolytic dependency. Loss of FGD5 sensitized PDAC cells to 2-DG, reduced clonogenic growth and stem-like properties, and was associated with a shift from glycolysis toward oxidative phosphorylation. Clinically, FGD5 expression was elevated in PDAC tissues and correlated with unfavorable patient outcomes. Mechanistically, FGD5 interacted with and stabilized PGK1 by limiting STUB1-mediated ubiquitination and proteasomal degradation. Pharmacological perturbation with CB-5083, a compound prioritized through structure-guided screening, modulated FGD5-PGK1-associated proteostasis readouts, increased PGK1 ubiquitination, reduced PGK1 abundance, and cooperated with 2-DG to suppress PDAC growth in vitro and in vivo. Moreover, lactate-associated H3K18 histone lactylation was linked to increased FGD5 transcription, consistent with a feed-forward regulatory connection between glycolysis, epigenetic modification, and metabolic adaptation. Collectively, our findings position FGD5 as a metabolic vulnerability in PDAC and provide a mechanistic framework supporting combinatorial strategies that couple glycolysis inhibition with perturbation of FGD5-PGK1-associated proteostasis. A genome-wide CRISPR-Cas9 screen identified FGD5 as a metabolic vulnerability that increases PDAC sensitivity to the glycolysis inhibitor 2-deoxy-D-glucose (2-DG). In PDAC cells, FGD5 interacts with PGK1 and supports PGK1 stability by limiting STUB1-dependent ubiquitination and proteasomal degradation, thereby sustaining aerobic glycolysis and lactate production. Glycolysis-derived lactate is associated with increased H3K18 histone lactylation (H3K18la) at the FGD5 promoter, accompanied by elevated FGD5 transcription, consistent with a metabolic-epigenetic regulatory link. Pharmacological perturbation with CB-5083 attenuates FGD5-PGK1-associated proteostasis readouts, whereas 2-DG inhibits glycolytic flux and lactate-associated H3K18la. Together, CB-5083 and 2-DG cooperate to suppress PDAC growth by coupling perturbation of the FGD5-PGK1-associated proteostasis axis with glycolytic inhibition. - Source: PubMed
Publication date: 2026/08/07
Song WentingLuo JianongCai KunChen ShiyuRan SuyeJiang XueyiYu ChaoSun Chengyi