Ask about this productRelated genes to: USP39 antibody
- Gene:
- USP39 NIH gene
- Name:
- ubiquitin specific peptidase 39
- Previous symbol:
- -
- Synonyms:
- SAD1, CGI-21, SNRNP65
- Chromosome:
- 2p11.2
- Locus Type:
- gene with protein product
- Date approved:
- 2003-09-04
- Date modifiied:
- 2015-08-26
Related products to: USP39 antibody
Related articles to: USP39 antibody
- RIG-I and STING are critical for mediating the RIG-I and cGAS-STING signaling pathways that guard against viral infection. Here, we report that ubiquitin-specific peptidase 39 (USP39) positively regulates the RIG-I and cGAS-STING pathways to induce antiviral innate immunity in vitro and in vivo. The USP39 deficiency impaired the antiviral immune response of macrophages, leading to low type I IFNs expression, and high RNA and (e.g., VSV, H1N1 PR8) DNA virus (e.g., HSV-1) replication. Moreover, USP39-deficient mice were more sensitive to VSV or HSV-1 infection than control mice. Conversely, USP39 overexpression promoted the antiviral immune response. Mechanistically, we found that USP39 regulates RIG-I protein expression by promoting pre-RIG-I mRNA splicing and maturation. In addition, we also revealed that USP39 interacts with and stabilizes STING protein by deubiquitinating K48-linked polyubiquitin of STING at K288. These data show that USP39 positively regulates RNA and DNA-virus-induced RIG-I and cGAS-STING signaling, respectively, by promoting post-transcriptional control of RIG-I and stabilization of STING. These data provide new insights and potential therapeutic targets to control viral infections. - Source: PubMed
Publication date: 2026/05/11
Quan JiazhengZhao XibaoChen ShaoyingLi HongruiChen WeiDi QianqianLi XunweiZhao JiajingWu HanChen JinXiao YueWu ZheruiChen Weilin - - Source: PubMed
Publication date: 2026/04/27
Yang JiwenLi ChengYin WeiliFang FangZhao Zhiyong - Ubiquitin-specific protease 39 (USP39) is a multifunctional protein that plays a pivotal role in cellular homeostasis and tumorigenesis by integrating ubiquitin-dependent regulation, a mechanism governing protein stability, function, and interactions via the ubiquitination system, with RNA splicing. Although categorized within the deubiquitinating enzyme (DUB) USP family, USP39 exhibits markedly reduced canonical enzymatic activity due to structural alterations in its conserved cysteine-histidine catalytic motif. Instead, it engages in biological processes through non-catalytic mechanisms, such as zinc finger domain-mediated spliceosome assembly and non-classical deubiquitination to stabilize oncoproteins. As a key regulator of pre-mRNA splicing, the cell cycle (particularly the G2/M transition), and tumorigenesis, USP39 dysregulation is closely associated with cancer proliferation, metastasis, and chemoresistance. Emerging research on USP39's dual roles in deubiquitination and RNA splicing regulation has established it as a central hub molecule in cancer biology. This article systematically reviews the structural uniqueness, dual regulatory functions, and pathological implications of USP39, highlighting its potential as both a biomarker and therapeutic target. These insights aim to inform the development of novel strategies for tumor diagnosis and treatment. - Source: PubMed
Publication date: 2026/03/27
Yu XinYao MingyuZheng XuecongSong QinghangWang MengjunHe YangfanLi BingLiu Chunyan - Intervertebral disc degeneration (IVDD) is a leading cause of chronic low back pain. Programmed cell death, particularly necroptosis, contributes to nucleus pulposus (NP) cell loss. Mixed lineage kinase domain-like protein (MLKL) phosphorylation plays a critical role in necroptotic execution, but its upstream regulation in IVDD remains poorly defined. - Source: PubMed
Publication date: 2026/01/12
Zhu ZhenyuLin XiaofengKong FanqiWang ZiranLiang YongchengJi ChenglongChen HongxuanSun KaiqiangWang ChangnanXu XimingShi Jiangang - Increasing evidences demonstrate that mitochondrial function is essential for cancer cell survival and metastasis. However, the role of mitochondrial metabolic reprogramming in ovarian cancer progression remains largely unknown. Here, we report that mitochondrial chaperone BCS1L generates two major alternative-spliced isoforms, a full-length isoform (BCS1L-L) and a short isoform lacking exon 2 (BCS1L-S). Interestingly, BCS1L-L is elevated in several human cancers, and it significantly increased oxidative phosphorylation and ATP production in the present work, which is required for the survival of cancer cells. In contrast, BCS1L-S was unable to localize to the mitochondria as BCS1L-L did, and this led to impaired metabolic function. Mechanistically, splicing factor USP39 promoted exon 2 inclusion, thus facilitating the generation of oncogenic BCS1L-L and, thereby, maintaining mitochondrial homeostasis and survival of ovarian cancer cells. Importantly, we developed splice-switch antisense oligonucleotides (ASOs) that successfully induced exon 2 skipping and decreased BCS1L-L abundance, resulting in impaired tumor growth. These findings suggest that targeting oncogenic BCS1L-L by ASOs is a novel approach for ovarian cancer treatment. - Source: PubMed
Publication date: 2026/03/03
Xu MeiningWang ZixiangYang SiyuanLi GaoyuanZhang XiyuZhao LingYang LeiQiu ChunhongFeng XianguangZhang KaiLiu BinWei Jian-JunLi YuliangLiu GangCui BaoxiaQin JunchaoLiu Zhaojian