Ask about this productRelated genes to: C6orf113 antibody
- Gene:
- ZUP1 NIH gene
- Name:
- zinc finger containing ubiquitin peptidase 1
- Previous symbol:
- C6orf113, ZUFSP
- Synonyms:
- dJ412I7.3
- Chromosome:
- 6q22.1
- Locus Type:
- gene with protein product
- Date approved:
- 2003-11-25
- Date modifiied:
- 2019-02-26
Related products to: C6orf113 antibody
Related articles to: C6orf113 antibody
- Olaparib resistance limits its therapeutic efficacy in triple-negative breast cancer (TNBC). Exploring the mechanisms underlying olaparib resistance and developing combination strategies are of great clinical significance for improving the long-term therapeutic benefit in TNBC. - Source: PubMed
Publication date: 2025/11/16
Huang ShanshanQiu YuWu LinyuXie YiHe ZhitingLi YingqingXie Xinhua - Zinc finger-containing ubiquitin peptidase 1 (ZUP1) is a protein characterized by four N-terminal zinc finger domains and a C-terminal deubiquitinase (DUB) domain. While it is associated with the DNA damage response, the role of ZUP1 in innate immunity remains unclear. Here, we identify ZUP1 as a crucial component of the mitochondrial antiviral signaling (MAVS) complex, essential for host antiviral defense. We show that viral infection significantly upregulates ZUP1 expression, and mice lacking ZUP1 exhibit impaired type I interferon (IFN) production and increased susceptibility to viral infection, as evidenced by higher mortality rates. This underscores the protective role of ZUP1 in host immunity. Mechanistically, ZUP1 binds to MAVS through its C-terminal domain independently of DUB activity. Instead, ZUP1 utilizes its zinc finger domains, particularly the third zinc finger, to directly bind viral RNA. This interaction enhances the association of ZUP1 with MAVS and promotes its aggregation on mitochondria during viral infection. ZUP1 also interacts with TBK1 and NEMO within the MAVS complex, facilitating IRF3 activation and type I IFN production. These findings establish ZUP1 as a zinc finger-containing regulator that amplifies MAVS-dependent antiviral immunity, linking viral RNA recognition to downstream signaling and highlighting potential targets for therapeutic intervention against viral infections. - Source: PubMed
Hao WenyanGuo MengfanJi XinZhao XuyangZhu MingluJin YanWang GuangxiFeng JiawenLu DanYin Yuxin - Mitochondria serve as a platform for innate immune signaling transduction, and mitochondrial antiviral signaling protein (MAVS) is essential for interferon-β (IFN-β) production and innate antiviral immunity against RNA viruses. Here, we identified zinc finger-containing ubiquitin peptidase 1 (ZUFSP/ZUP1) as a MAVS-interacting protein by using proximity-based labeling technology in HEK293T and found it could act as a positive regulator of the retinoic acid-inducible gene-I (RIG-I)-like receptors(RLRs), including RIG-I and interferon-induced helicase C domain-containing protein 1 (MDA5). ZUFSP deficiency markedly inhibited RNA virus-triggered induction of downstream antiviral genes, and Zufsp-deficient mice were more susceptible to RNA virus infection. After RNA virus infection,ZUFSP was translocated from cytoplasm to nucleus and interacted with chromatin remodeling complex to facilitate the opening of IFN-stimulated gene (ISG) loci for transcription. This study provides a critical mechanistic basis for MAVS-regulated chromatin remodeling to promote interferon signaling. - Source: PubMed
Publication date: 2024/03/08
Li TongyuLi Siji - The objective of this study was to screen lymphoma radiotherapy-resistant genes using CRISPR activation (CRISPRa). - Source: PubMed
Publication date: 2023/01/30
Luo Bi-HuaHuang Jian-QingHuang Chun-YuTian PanChen Ai-ZhenWu Wei-HaoMa Xiao-MeiYuan Yue-XingYu Lian - Eukaryotic deubiquitinases are important regulators of ubiquitin signaling and can be subdivided into several structurally distinct classes. The ZUFSP family, with ZUP1 as its sole human member, has a modular architecture with a core catalytic domain highly active against the ubiquitin-derived peptide RLRGG, but not against ubiquitin itself. Ubiquitin recognition is conferred by additional non-catalytic domains, making full-length ZUP1 active against long K63-linked chains. However, non-mammalian ZUFSP family members contain different ubiquitin-binding domains in their N-terminal regions, despite their high conservation within the catalytic domain. Here, by working with representative ZUFSP family members from insects, fungi and plants, we show that different N-terminal domains are associated with different linkage preferences. Biochemical and structural studies suggest that the acquisition of two family-specific proximal domains have changed the default K48 preference of the ZUFSP family to the K63 preference observed in ZUP1 and its insect homolog. Additional N-terminal zinc finger domains promote chain cleavage without changing linkage-specificity. - Source: PubMed
Publication date: 2022/01/20
Hermanns ThomasPichlo ChristianBaumann UlrichHofmann Kay