Ask about this productRelated genes to: STUB1 Blocking Peptide
- 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 Blocking Peptide
Related articles to: STUB1 Blocking Peptide
- The E3 ubiquitin ligase CHIP/STUB1 is a known tumor suppressor in colorectal cancer (CRC) and other malignancies, but its mechanistic role in metabolic reprogramming remains elusive. This study aimed to elucidate whether CHIP regulates glycolysis in CRC through targeting key metabolic enzymes. - Source: PubMed
Publication date: 2026/07/07
Li ChunyaKuang YanshenHou XinwenZhao LinpengZhang YutongWang ShaochangWang PeijiaDai ZifanWang XiaoxuanShang Yu - Cold exposure is an important environmental risk factor for adverse cardiovascular outcomes, but the immune mechanisms linking cold stress to myocardial injury remain incompletely defined. Here, we investigated whether curcumin protects the cold-stressed heart by regulating macrophage polarization and the STUB1/STAT1-STAT6-KLF4 signaling network. Using a severe intermittent mouse cold-exposure model and a mild hypothermic BMDM cold-mimic system, we found that cold stress impaired cardiac function, increased inflammatory infiltration, and shifted macrophages toward a pro-inflammatory phenotype. Cold mimicry enhanced STUB1-STAT1 interaction and K48-linked STAT1 ubiquitination, reduced STAT1 abundance, and was accompanied by suppression of STAT6 activation and KLF4 transcription. Given the canonical antagonism between STAT1- and STAT6-driven macrophage programs, these changes are interpreted as context-specific co-disruption of STAT-family signaling under cold-induced proteostatic/inflammatory stress, rather than as evidence that STAT1 degradation alone directly suppresses STAT6. Curcumin reduced STUB1 abundance and STUB1-STAT1 engagement, attenuated STAT1 ubiquitination, restored STAT6 nuclear signaling and STAT6-dependent Klf4 transcription, and promoted anti-inflammatory macrophage polarization. In a species-matched Transwell co-culture system, curcumin-treated macrophages reduced inflammatory cytokine release and improved cardiomyocyte viability through paracrine effects. Macrophage-specific Klf4 deletion markedly attenuated curcumin-mediated immune remodeling and cardioprotection in vivo. These findings identify a macrophage-centered signaling network that contributes to cold stress-induced myocardial injury and position curcumin as an experimental immunomodulatory candidate. However, direct curcumin-STUB1 target engagement, systemic cytokine changes, optimal dosing/formulation, and human efficacy remain to be established. - Source: PubMed
Publication date: 2026/06/19
Cong PeifangTong ChangciLiu JinpengLuo ZhonghuaLi HaikunYao JianLiu Yunen - Obesity is recognized as a key contributor to the impaired endometrial receptivity that results in infertility; however, the molecular mechanisms underlying endometrial dysfunction remain incompletely understood. In this study, proteomic and ubiquitination analyses of secretory-phase endometrial tissue revealed a significant upregulation of SNCA/synuclein alpha and dysregulation of macroautophagy/autophagy in women with obesity. SNCA is best known for its role in neurodegenerative protein aggregation disorders. Proteomic and ubiquitination analysis of secretory-phase endometrial tissue revealed a significant upregulation of SNCA and dysregulation of autophagy in women with obesity. This study aimed to elucidate the role and mechanistic basis of SNCA and autophagy in obesity-associated endometrial receptivity defects. We demonstrated that elevated SNCA expression in endometrium and endometrial stromal cells (ESCs) correlated with impaired autophagy and disrupted decidualization in and . Mechanistically, SNCA directly interacted with the E3 ubiquitin ligase STUB1 (STIP1 homology and U-box containing protein 1) in ESCs, thereby disrupting the association between STUB1 and phosphorylated TFEB (transcription factor EB; p-TFEB). This interaction attenuated p‑TFEB degradation, leading to suppressed autophagic flux and ultimately compromised decidualization of ESCs. Conversely, knockout alleviated obesity-induced endometrial impairments in mice. Moreover, STUB1 overexpression rescued decidualization and autophagy defects. Notably, metformin intervention restored autophagic activity and endometrial receptivity in obese mice by downregulation of SNCA independent of its autophagy-modulating effects. Together, these findings uncovered a novel pathogenic mechanism in which obesity-driven SNCA overexpression impairs endometrial receptivity by inhibiting STUB1-TFEB-mediated autophagy, positioning the SNCA-STUB1-TFEB axis as a promising therapeutic target for obesity-related endometrial infertility.: BECN1: beclin 1; CCK-8: Cell Counting Kit-8; CQ: chloroquine; DEPs: differentially expressed proteins; DIO: diet-induced obese; ESCs: endometrial stromal cells; FBS: fetal bovine serum; GD7: gestational day 7; GSEA: Gene Set Enrichment Analysis; HFD: high-fat diet; HOXA10: homeobox A10; IGFBP1: insulin like growth factor binding protein 1; IPGTT: intraperitoneal glucose tolerance test; LIF: LIF interleukin 6 family cytokine; PBS: phosphate-buffered saline; PRL: prolactin; Rapa: rapamycin; SNCA/synuclein alpha; SQSTM1/p62: sequestosome 1; STUB1: STIP1 homology and U-box containing protein 1; TC: total cholesterol; TEM: transmission electron microscopy; TFEB: transcription factor EB; UPS: ubiquitin-proteasome system; WOI: window of implantation. - Source: PubMed
Publication date: 2026/06/23
Tang FeiGuo PeipeiWang LitingXie PengxiangWang YiWang YueFang YouyanLi CaihuaCao YunxiaXiang HuifenYin ZongzhiZhang DongWei ZhaolianHe Ye - African swine fever virus (ASFV) primarily invades through the respiratory and intestinal mucosa, where type III interferons (IFN-λ) play a pivotal role in local immunity. However, whether ASFV counteracts this IFN-λ-mediated antiviral defense remains largely unknown. Here, we demonstrate that ASFV infection dampens IFN-λ production, where the viral protein pM448R serves as a suppressor. Mechanistically, pM448R targets interferon regulatory factor 1 (IRF1) for proteasomal degradation by recruiting the E3 ubiquitin ligase STIP1 homology and U box-containing protein 1 (STUB1), which catalyzes K48-linked ubiquitination of IRF1. Moreover, infection with the M448R-deficient ASFV mutant leads to increased IRF1 protein stability and elevated expression of IRF1 target genes, including OAS1, OAS2, and ZBP1. Our findings reveal a novel immune evasion strategy whereby ASFV hijacks the host ubiquitin-proteasome system to degrade IRF1, thereby subverting IRF1-dependent transcriptional programs, including IFN-λ induction, to facilitate mucosal invasion.IMPORTANCEAfrican swine fever virus (ASFV) remains a major threat to the global swine industry. However, how the virus evades mucosal innate immunity at its portal of entry remains poorly understood. The transcription factor IRF1 serves as a central hub in mucosal antiviral defense, coordinating the expression of IFN-λ and numerous other restriction factors. In this study, we identify pM448R as a viral antagonist that directs IRF1 for ubiquitin-mediated degradation, which reveals a novel mechanism by which ASFV destroys the mucosal immune barrier. These findings not only deepen our understanding of viral interference with IRF1-dependent defense pathways, but also provide potential insights for the development of live-attenuated vaccines. - Source: PubMed
Publication date: 2026/06/09
Zhao JinyuXie JiaxuShi YuxinMou ChunxiaoChen Zhenhai - Human coronaviruses (HCoVs) are a group of RNA viruses characterized by high genetic variability and cross-species transmission potential. They can cause a wide spectrum of respiratory illnesses, ranging from mild upper respiratory tract infections to severe pneumonia, and acute respiratory distress syndrome. PTEN, a well-known tumor suppressor, not only plays a crucial role in tumorigenesis but also enhances antiviral immunity by regulating IRF3 phosphorylation and promoting type I interferon production. In this study, we observed that PTEN significantly inhibited the replication of various HCoVs, including SARS-CoV-2, HCoV-229E, and HCoV-OC43. However, SARS-CoV-2 infection antagonizes the antiviral function of PTEN. Mechanistically, PTEN undergoes ubiquitination at lysine 6, followed by proteasomal degradation after SARS-CoV-2 infection. Through screening, it was found that STUB1 is the key E3 ligase responsible for PTEN degradation under SARS-CoV-2 infection. Furthermore, screening of SARS-CoV-2-encoded proteins revealed that ORF3a promotes STUB1-mediated PTEN ubiquitination and degradation at K6. Previous studies have shown that Oroxin B can exert the effect of a PTEN agonist by upregulating the expression of PTEN. In this study, we demonstrated that Oroxin B significantly enhances antiviral responses in mice. In conclusion, this study reveals the molecular mechanism by which SARS-CoV-2 evades PTEN-mediated antiviral effects, providing new insights for the development of PTEN-targeted antiviral strategies. - Source: PubMed
Publication date: 2026/06/02
Fan LujieGao XiangFeng WeiHuang QiangWei XiafeiYang ChuweiWu YeziShen XiaotongZhao JuanjuanZhou YuzhengZhang Zheng