Ask about this productRelated genes to: RNF31 Blocking Peptide
- Gene:
- RNF31 NIH gene
- Name:
- ring finger protein 31
- Previous symbol:
- -
- Synonyms:
- ZIBRA, FLJ10111, FLJ23501, HOIP, Paul
- Chromosome:
- 14q12
- Locus Type:
- gene with protein product
- Date approved:
- 2003-09-29
- Date modifiied:
- 2019-04-23
Related products to: RNF31 Blocking Peptide
Related articles to: RNF31 Blocking Peptide
- Inflammatory bowel disease (IBD) is characterized by impaired autophagy and chronic inflammation. Although the E3 ubiquitin ligase RNF31 is upregulated in IBD, its pathogenic mechanisms remain incompletely understood. To address this, a combination of in vitro and in vivo methods was employed. In vitro, lipopolysaccharide (LPS)-stimulated cell models were used to analyze transcription factor EB (TFEB) phosphorylation, its interaction with RNF31, ubiquitination, and subcellular localization. In vivo, a DSS-induced IBD mouse model was used to assess intestinal pathology, inflammation, and RNF31-TFEB-NLRP3 axis proteins after treatment with a novel synthetic curcumin analog (CM-C1). We identified TFEB as a novel substrate of RNF31. LPS-induced phosphorylation of TFEB promoted its binding to RNF31 (via TFEB-S281/T276 and RNF31-K908), leading to TFEB ubiquitination, proteasomal degradation, suppressed autophagy, and subsequent NLRP3 inflammasome activation. The bioavailable TFEB activator CM-C1 directly disrupted the RNF31-TFEB interaction. This action promoted TFEB nuclear translocation, restored autophagic flux, alleviated intestinal inflammation in vitro and in vivo, and beneficially remodeled the gut microbiota. Our study unveils the RNF31-TFEB-NLRP3 axis as a pivotal pathogenic pathway in IBD and nominates CM-C1, which targets this axis, as a promising multimodal therapeutic candidate. - Source: PubMed
Publication date: 2026/05/23
Han LuXie YangZeng ChunyanChen Youxiang - The deubiquitinating enzyme OTULIN has been implicated in the development of lung injury, and regulating its expression may either exacerbate or alleviate pulmonary inflammatory damage. In this study, we aimed to investigate the role of deubiquitinating enzyme OTULIN in hyperoxia-induced lung injury and the underlying mechanisms involved. A bronchopulmonary dysplasia (BPD) model was established by exposing neonatal mice to a hyperoxic environment, and the effects of regulating OTULIN expression on mitochondrial homeostasis in pulmonary epithelial cells were further examined under hyperoxic conditions. In addition, we investigated the mechanisms through which OTULIN regulates mitochondrial-associated proteins and the ubiquitination mechanisms of differential mitochondrial protein OPA1. The results showed that hyperoxia induced significant lung injury in neonatal mice and was accompanied by upregulation of OTULIN expression. Additionally, hyperoxia disrupted mitochondrial homeostasis in neonatal mice lung tissue, as observed by a reduction in mitochondrial number and increased mitochondrial fusion and autophagy. After hyperoxia exposure, overexpression of OTULIN significantly reduced mitochondrial reactive oxygen species (ROS) levels in alveolar epithelial cells, maintained mitochondrial membrane potential, and promoted mitochondrial homeostasis. Mechanistically, OTULIN was found to directly interact with OPA1 and regulate its ubiquitination status. The E3 ubiquitin ligase RNF31 was identified as a key regulator of OPA1 stability, with knockdown of RNF31 reducing OPA1 levels. Moreover, OTULIN regulated the expression of both OPA1 and RNF31 and affected the stability of OPA1 and mitochondrial function through RNF31-dependent mechanisms. In vivo experiments further showed that knockdown of OTULIN aggravated hyperoxia-induced lung injury in neonatal mice, characterized by alveolar simplification, increased fibrosis, and further impairment of mitochondrial function, whereas overexpression of OTULIN alleviated these pathological changes. In conclusion, deubiquitinating enzyme OTULIN protected hyperoxia-induced neonatal lung injury and modulates mitochondrial protein OPA1 in association with the E3 ubiquitin ligase RNF31. These findings provide new insights into the pathogenesis of BPD and highlight the therapeutic potential of targeting the OTULIN/RNF31-OPA1 axis. - Source: PubMed
Publication date: 2026/05/30
Huang LiLiu QingZhang AiminLiu YanhanHuang FurongWang JuanmeiTan MantingWang DuaneZhao MenghuaWu Xu - The early detection and diagnosis of head and neck squamous cell carcinoma (HNSCC) pose significant challenges. - Source: PubMed
Publication date: 2026/04/24
Xia YichaoLou HuiquanShao ShengjieLiu XiangLi Yongsheng - Defensins, small cationic peptides with strong antimicrobial activity, are key effectors of innate immunity. α-defensins, human neutrophil peptides, are produced primarily by neutrophils and serve as an essential component of the airway defense system against invading pathogens. However, accumulating evidence indicates that α-defensins released from human neutrophils are markedly elevated in various lung diseases, where excessive α-defensins exert cytotoxic effects on epithelial and immune cells. - Source: PubMed
Publication date: 2026/01/20
Lee JungnamMohammad NaweedMun SeyoungHan KyudongFlagg-Dowie TammyMagallon MariaBrantly Mark LSerban Karina A - Transverse tubules (T-tubules) are invaginations of the muscle plasma membrane that facilitate rapid transmission of action potentials, ensuring synchronized muscle contraction. Despite their essential role in muscle physiology, the mechanisms underlying T-tubule formation remain elusive. Here, we identify LUBEL/RNF31, a ubiquitin E3 ligase responsible for linear (M1-linked) ubiquitination, as a key regulator of T-tubule biogenesis in . Loss of LUBEL leads to Amphiphysin (Amph)-positive membrane sheets instead of tubular networks. The ubiquitin ligase activity of LUBEL and direct interaction with Amph, a BAR domain protein involved in membrane tubulation, are crucial for proper T-tubule morphology. LUBEL and M1-linked ubiquitin chains assemble into puncta on membranes through multivalent interactions, facilitating Amph-mediated tubulation. Notably, the Amph-LUBEL/RNF31 interaction is evolutionarily conserved across species, underscoring a fundamental role for linear ubiquitination in membrane remodeling. Our findings uncover an unexpected function of linear ubiquitination in membrane deformation driven by BAR proteins. - Source: PubMed
Publication date: 2026/01/07
Kawaguchi KoheiHama YutaroYoshikawa HarunoriNishino KoheiMorimoto KazukiNakamura TsuyoshiKoizumi MichikoSakamaki YurikoAbe KotaKakuta SoichiroIchimura KoichiroIkeda FumiyoKosako HidetakaFujita Naonobu