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
- Diabetic kidney disease (DKD) is a leading cause of chronic kidney disease, and tubulointerstitial fibrosis (TIF) represents its final pathological hallmark. Progestin and adipoQ receptor 3 (PAQR3) has been implicated in metabolism and inflammation, but its role in DKD remains largely unexplored. Here, we report that PAQR3 expression is markedly upregulated in the kidneys of STZ-induced diabetic mice and in high glucose-stimulated NRK-52E tubular epithelial cells, correlating with the onset of tubular epithelial-mesenchymal transition (EMT) and fibrosis. Functional studies demonstrated that PAQR3 overexpression via AAV delivery in db/db mice significantly exacerbated renal dysfunction, fibrotic lesions, and EMT, whereas PAQR3 knockdown in cultured tubular cells attenuated the EMT phenotype. Mechanistically, PAQR3 selectively increased NOX4 protein levels without affecting its mRNA expression, leading to enhanced ROS production and oxidative stress. Notably, PAQR3 suppressed STUB1-mediated NOX4 ubiquitination, thereby stabilizing NOX4 protein. Collectively, these findings suggest that PAQR3 modulates NOX4 protein stability by suppressing its ubiquitination and the PAQR3-STUB1-NOX4 axis may contribute to TIF progression in DKD. - Source: PubMed
Publication date: 2026/09/26
Sun XiaohongTan ShiyunWu JiabiWang LirongWang Shaogui - Epidermal homeostasis relies on the precise balance between the self-renewal and differentiation of basal keratinocytes, a process highly dependent on the fidelity of cell division and centrosome function. However, the molecular mechanism regulating this process remains poorly understood. Here, we identify protein arginine methyltransferase 1 (PRMT1) as a crucial orchestrator of epidermal homeostasis. Genetic ablation of in mice causes severe epidermal hyperplasia characterized by aberrant expansion of the stratum basale and disruption of the mitotic fidelity of basal cells. Mechanistically, PRMT1 directly interacts with and catalyzes the asymmetric arginine dimethylation of the centrosomal OFD1/FOR20-interacting protein (OFIP) at arginine 50. This methylation is required for the subsequent recognition and ubiquitination of OFIP by the E3 ubiquitin ligase STUB1. Consequently, PRMT1 deficiency prevents OFIP methylation and degradation, resulting in its dramatic accumulation at the centrosome. This buildup drives aberrant centrosome overduplication and the formation of multipolar spindles, ultimately compromising the integrity of epidermal renewal. Our findings delineate the PRMT1-OFIP-STUB1 axis as a mechanistic framework governing centrosome numerosity and epidermal homeostasis, advancing understanding of cutaneous barrier integrity and providing a potential therapeutic target for dermatopathological conditions. - Source: PubMed
Publication date: 2026/09/23
Liu KaiSong TingZhao JunkuiYan ShaodongBu WeiwenZhang ShenyingHu DieLi DengwenZhao HuijieZhou Jun - Association between monoallelic STUB1 variant and expanded ATXN8OS alleles was recently reported, suggesting a pathogenic interaction that may influence spinocerebellar ataxia type 48 (SCA48) phenotype. - Source: PubMed
Publication date: 2026/09/21
Mouraux CharlotteMéreaux Jean-LoupDavoine Claire-SophieNoel Léna GuillotPetit EmilienThomas QuentinNasraoui AdemHeinzmann AnnaEwenczyk ClaireBrice AlexisDurr AlexandraCoarelli Giulia - - Source: PubMed
Publication date: 2026/09/21
Yamada KazukiOgata ShunsukeYaguchi HiroakiFujii ShintaroNomura TaichiKudo AkihikoEguchi KatsukiUwatoko HisashiShirai ShinichiTakahashi-Iwata IkukoMatsushima MasaakiHamanaka KoheiMiyatake SatokoNishino IchizoGoto Yu-IchiMatsumoto NaomichiYabe Ichiro - The Regulator of Cullins 1 (ROC1) or RING box protein-1 (RBX1) is an essential component of the largest multiunit Cullin-RING ubiquitin ligase (CRL). Previous studies demonstrated that ROC1 is frequently overexpressed in multiple malignancies, which predicts advanced cancer stages and poor prognosis. However, the molecular mechanisms driving ROC1 overexpression in cancers remain largely unknown. Herein, we reveal that HSP90 binds to ROC1 with its N-Terminus, thus promoting ROC1 stabilization. HSP90 inhibition with the N-Terminal, but not the C-Terminal inhibitors accelerate ROC1 destabilization by facilitating its ubiquitination and subsequent degradation by CHIP E3 ligase. CHIP specifically interacts with ROC1 at its CC domain, thus promoting the K48-linked-ubiquitin-mediated degradation of ROC1 at the K26 residue. Indeed, deletion of CHIP markedly blocks HSP90-inactivation-induced ROC1 reduction. Function exploration reveals that HSP90 inhibition suppresses lung adenocarcinoma (LUAD) cell growth substantially by decreasing ROC1 abundance. In clinic, HSP90β and ROC1 are overexpressed in LUAD samples, which have positive correlation and predict poor prognosis of LUAD patients. LUAD organoids analysis reveals that HSP90 blockage promotes ROC1 destabilization and inhibits the growth of organoid cells. Taken together, the present results demonstrate the regulatory mechanism of ROC1 in malignancies and suggest a novel mechanism of the oncogenic role of HSP90 to promote lung tumorigenesis. - Source: PubMed
Publication date: 2026/09/21
Li LihuiZhang YingLi MengYang XuhuiChang GailiZhang WenjuanYan YuerenPan YunjianLiang YupeiWang ShiwenWang MingsongHoffman Robert MWei WenyiJia Lijun