Ask about this productRelated genes to: RNF167 antibody
- Gene:
- RNF167 NIH gene
- Name:
- ring finger protein 167
- Previous symbol:
- -
- Synonyms:
- DKFZP566H073
- Chromosome:
- 17p13.2
- Locus Type:
- gene with protein product
- Date approved:
- 2004-07-29
- Date modifiied:
- 2016-10-05
Related products to: RNF167 antibody
Related articles to: RNF167 antibody
- Mucopolysaccharidosis type II, also known as Hunter syndrome, is a rare and fatal disease caused by mutations in the iduronate 2-sulfatase (IDS) encoding gene. Enzymatically inactive IDS variants lead to pathological accumulation of glycosaminoglycans in lysosomes, resulting in dysfunction of multiple organs. IDS is expressed as a precursor protein, and its proper processing and lysosomal targeting are crucial for enzymatic activity. However, the intracellular dynamics of IDS remain poorly understood, and a better understanding of its processing mechanisms would benefit the development of new therapeutic strategies. alphafold 3 predicted an interaction between IDS and the E3 ubiquitin ligase RNF13. Co-immunoprecipitation assays confirmed this interaction and further revealed that RNF13 preferentially interacts with a predominantly underglycosylated immature form of IDS, leading to altered IDS glycosylation and maturation. The results demonstrate that IDS glycosylation site Asn246 is important for lysosomal targeting, although its glycosylation is not altered by RNF13. Importantly, this study demonstrates that RNF13 forms a heterodimer with the E3 ubiquitin ligase RNF167, which modulates the lysosomal trafficking of both proteins. In addition, the heterodimer interacts and alters IDS processing differently than RNF13 or RNF167 alone. RNF13 catalytic E3 ligase activity is required to generate an underglycosylated form, but not that of RNF167. This study shows that the proteasome rapidly degrades IDS underglycosylated forms, and RNF13 exerts a protective effect. Overall, this study reveals a previously undescribed and dual role of RNF13 in IDS maturation and degradation, providing mechanistic insights into IDS trafficking. - Source: PubMed
Publication date: 2025/12/12
Cabana Valérie CBouchard Antoine YSénécal Audrey MCappadocia LaurentLussier Marc P - This study investigates the role of ubiquitination-related genes in pancreatic cancer (PC) using single-cell RNA sequencing (scRNA-seq), spatial transcriptomics, and multi-omics approaches. scRNA-seq data (GSE155698) from PC samples identified 12 cell types, with endothelial cells exhibiting high ubiquitination scores (High_ubiquitin-Endo) and enriched interactions with fibroblasts/macrophages via WNT, NOTCH, and integrin pathways. Spatial transcriptomics (GSE235315) validated cell-type localization. Mendelian randomization (SMR) analysis prioritized TRIM9 as a PC-protective gene, downregulated in tumors and correlated with better survival. WGCNA revealed TRIM9-co-expressed modules linked to prognosis. A machine learning-based prognostic model (CoxBoost+RSF) integrating seven genes (TSPAN6, TSC1, RNF167, PBXIP1, LRRC49, KATNAL2, IGF2BP2) stratified patients into high/low-risk groups with distinct survival, mutation burdens, and immune infiltration. TRIM9 overexpression suppressed PC cell proliferation/migration , while knockdown enhanced malignancy. Mechanistically, TRIM9 promoted K11-linked ubiquitination and proteasomal degradation of HNRNPU, dependent on its RING domain. , TRIM9 overexpression reduced tumor growth, rescued by HNRNPU co-expression. Integrated analyses highlight TRIM9 as a tumor suppressor and prognostic biomarker, mediated via ubiquitination-dependent regulation of HNRNPU stability. This work provides insights into ubiquitination-driven PC pathogenesis and therapeutic targeting. - Source: PubMed
Publication date: 2025/09/19
Chen LiangYing XiaomeiMa ChenfengTang QikaiChen Shuai - Gastric cancer (GC) continues to pose a significant global health burden, necessitating a thorough understanding of the molecular mechanisms driving its progression. This study aimed to investigate the regulatory role of SMAD3 in modulating Sestrin2 ubiquitination stability and its implications in GC cell behaviors. - Source: PubMed
Publication date: 2025/08/01
Zhang NingZhao NaZhang HainanYao LeSi Hongtao - The precise regulation of the RIG-I-like receptors (RLRs)-mediated type I interferon (IFN-I) activation is crucial in antiviral immunity and maintaining host immune homeostasis in the meantime. Here, we identify an E3 ubiquitin ligase, namely RNF167, as a negative regulator of RLR-triggered IFN signaling. Mechanistically, RNF167 facilitates both atypical K6- and K11-linked polyubiquitination of RIG-I/MDA5 within CARD and CTD domains, respectively, which leads to degradation of the viral RNA sensors through dual proteolytic pathways. RIG-I/MDA5 conjugated with K6-linked ubiquitin chains in CARD domains is recognized by the autophagy cargo adaptor p62, that delivers the substrates to autolysosomes for selective autophagic degradation. In contrast, K11-linked polyubiquitination in CTD domains leads to proteasome-dependent degradation of RLRs. Thus, our study clarifies a function of atypical K6- and K11-linked polyubiquitination in the regulation of RLR signaling. We also unveil an elaborate synergistic effect of dual proteolysis systems to control amplitude and duration of IFN-I activation, hereby providing insights into physiological roles of the cross-talk between these two protein quality control pathways. - Source: PubMed
Publication date: 2025/02/24
He MiaoYang ZixiaoXie LuyangChen JunhaiLiu ShuruiLu LiaoxunLi ZiboZheng BirongYe YuLin YuxinBu LangXiao JingshuZhong YonghengJia PenghuiLi QiangLiang YinmingGuo DeyinLi Chun-MeiHou Panpan - This study investigated modifications to the ubiquitin proteasome system (UPS) in a mouse model of type 2 diabetes mellitus (T2DM) and their relationship to heart complications. mice heart tissues were compared with mice tissues using RNA sequencing, qRT-PCR, and protein analysis to identify cardiac UPS modifications associated with diabetes. The findings unveiled a distinctive gene profile in the hearts of mice with decreased levels of mRNA and increased levels of , indicating potential cardiac dysfunction. The mRNA levels of (deubiquitinating enzyme), , and (proteasome β-subunits) were down-regulated in mice, while the mRNA levels of RNF167 (E3 ligase) were increased. Corresponding LMP2 and LMP7 proteins were down-regulated in mice, and RNF167 was elevated in diabetic mice. The reduced expression of LMP2 and LMP7, along with increased RNF167 expression, may contribute to the future cardiac deterioration commonly observed in diabetes. This study enhances our understanding of UPS imbalances in the hearts of diabetic mice and raises questions about the interplay between the UPS and other cellular processes, such as autophagy. Further exploration in this area could provide valuable insights into the mechanisms underlying diabetic heart complications and potential therapeutic targets. - Source: PubMed
Publication date: 2023/10/19
Nahum-Ankonina OrtalKurtzwald-Josefson EfratCiechanover AaronWaldman MaayanShwartz-Rohaker OrnaHochhauser EdithMeyer Sam JAravot DanPhillip MosheBarac Yaron D