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
- 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 - Spinal cord injury (SCI) is a severe traumatic condition with limited treatments. Ferroptosis, an iron-dependent type of controlled cell death, participates in SCI pathology. Nonetheless, the molecular mechanisms governing ferroptosis after SCI remain incompletely understood. Therefore, this study aims to elucidate the regulatory role of SIRT6 in neuronal ferroptosis post-SCI, identify its upstream modulator and downstream target, and evaluate the therapeutic potential of targeting this pathway for functional recovery. - Source: PubMed
Publication date: 2026/07/14
Wang ZhuanghuiYe WuWang JiaxingGe XuhuiZhu YufengLiu WeiMa QinghongCai WeihuaRong Yuluo