Ask about this productRelated genes to: UBE4A antibody
- Gene:
- UBE4A NIH gene
- Name:
- ubiquitination factor E4A
- Previous symbol:
- -
- Synonyms:
- UBOX2, UFD2, KIAA0126, E4
- Chromosome:
- 11q23.3
- Locus Type:
- gene with protein product
- Date approved:
- 2000-01-28
- Date modifiied:
- 2016-11-09
Related products to: UBE4A antibody
Related articles to: UBE4A antibody
- Viperin is considered as an antiviral protein known to directly target a variety of viruses. However, whether and how Viperin affects virus infection by targeting intracellular immune signaling remain unexplored. Here, we reveal that Viperin inhibits type-I interferon (IFN-I) antiviral immune signaling by degrading STAT1. We found that IFN-I upregulates the ubiquitin E3 ligase ITCH to degrade UBR5, while Viperin subsequently recruits another ubiquitin E3 ligase UBE4A to promote STAT1 ubiquitination and degradation to attenuate IFN-I signaling. Moreover, the multifunctional interfering peptide VS-IP1 can block Viperin-mediated STAT1 degradation, thus enhancing IFN-I antiviral immune function. This study reveals that Viperin is a suppressor of IFN-I immune signaling, which could renew understanding of the biological function of Viperin, and provide a strategy for enhancing clinical IFN-I therapeutic efficacy. - Source: PubMed
Publication date: 2026/04/03
Miao YingYuan YukangQian LipingYu YongCui QunZhang TingtingZhang RenxiaZhao QianLi ZhizeMiao AnningLi YanouWang JunXiong SidongZheng Hui - - Source: PubMed
Zhang Ming-PengSong ZaozhiZhang Wei-SanTan JinZhao Ming-HuiLian Lin-JuanCai Jie - There is compelling evidence that TNF preferentially activates and expands CD4Foxp3 regulatory T cells (Tregs) through TNFR2. However, the precise mechanisms underlying TNF-TNFR2 pathway-mediated Treg proliferation remain to be fully elucidated. In this study, using RNA-seq profiling of TNFR2 and TNFR2-deficient Treg cells, we identified that Trip13 is required for promoting TNF-TNFR2 pathway-mediated Treg expansion. Mechanistically, TRIP13 inhibited UBE4A-mediated ubiquitination degradation of HAT1 by directly binding to HAT1, thereby competing with UBE4A and promoting Treg expansion. In addition, TRIP13's ATPase activity was essential for its binding to HAT1, which promoted Treg expansion by increasing Foxp3 expression. In a mouse colitis model, TRIP13 overexpression markedly alleviated colon inflammation by enhancing Treg expansion, an effect that was reversed by HAT1 knockdown. Conversely, genetic ablation of TRIP13 substantially reversed the effects induced by HAT1 overexpression, including enhanced Treg expansion and attenuation of colitis. These findings illustrate the TRIP13/HAT1 axis-mediated mechanism for TNF-TNFR2-induced Treg expansion and indicate that targeting TRIP13 may offer therapeutic potential for autoimmune and inflammatory diseases. - Source: PubMed
Publication date: 2026/01/14
He TianzhenZhao LiwenFeng Chu-TingZhao Li-YaJing ShengnanYang HanWang KeYe SiyuZhao YingchunYu YingFu ZhutingChou Chon-KitChen XinGao Yong-Jing - Ubiquitin-dependent signaling is essential for maintaining intestinal homeostasis and its dysregulation contributes to chronic intestinal disorders, such as Inflammatory Bowel Disease (IBD). Ube4A is a U-box E3/E4 ubiquitin ligase involved in lipid metabolism and insulin signaling in metabolic tissues. Autoantibodies against Ube4A have been identified in patients with IBD and are associated with disease long-term complications. Despite these clinical associations, the physiological role of Ube4A in the gastrointestinal tract remains unknown. This study aimed to define the function of Ube4A in the colon and determine how its loss influences susceptibility to experimental colitis. - Source: PubMed
Publication date: 2026/01/03
Guignard SimonChakraborty MoleeGonzalez-Nieves SilviaDeBruin DavidEbert EmilyVinogradskaia AnastasiiaBrennan MichelleTeague Ryan MChakraborty AnutoshCifarelli Vincenza - Osteosarcoma (OS) is the most common primary bone tumor. Insulin Growth Factor-2 Binding Protein 3 (IGF2BP3) regulates mRNA stability and is a potential oncogene in many cancers, but its role in OS remains unknown. - Source: PubMed
Publication date: 2025/08/14
Li ShuoWang TianyangWang ErjianLin LinZhong Wei