TRIM25 (C-Terminus) Peptide
- Known as:
- TRIM25 (C-Terminus) Peptide
- Catalog number:
- 4315P
- Product Quantity:
- 0.05 mg
- Category:
- -
- Supplier:
- Prosci
- Gene target:
- TRIM25 (C-Terminus) Peptide
Related genes to: TRIM25 (C-Terminus) Peptide
- Gene:
- TRIM25 NIH gene
- Name:
- tripartite motif containing 25
- Previous symbol:
- ZNF147
- Synonyms:
- EFP, RNF147
- Chromosome:
- 17q23.1
- Locus Type:
- gene with protein product
- Date approved:
- 1994-03-16
- Date modifiied:
- 2015-09-01
Related products to: TRIM25 (C-Terminus) Peptide
Related articles to: TRIM25 (C-Terminus) Peptide
- Fibrosis represents a complex pathological process that culminates in organ damage and failure. Cataract, specifically anterior subcapsular cataract (ASC) and posterior capsular opacity (PCO), is a common manifestation of ocular fibrosis, primarily driven by the epithelial mesenchymal transition (EMT) of lens epithelial cells (LECs). Tripartite motif containing 25 (TRIM25), an E3 ubiquitin ligase and member of the TRIM protein family, plays a pivotal role in various biological processes including protein homeostasis, signaling pathways, immune responses, and cell growth. This study aims to elucidate the role of TRIM25 in LECs EMT and its underlying molecular mechanisms, thereby identifying a novel therapeutic target for the prevention and treatment of fibrotic cataracts. - Source: PubMed
Publication date: 2026/05/15
Liu YifanHuang YihanChen AnlinHan LeiBian LiXu XuanLi Yue - Ferroptosis, a unique form of regulated cell death induced by iron-dependent lipid peroxidation, has been implicated in the pathogenesis of Mycobacterium tuberculosis (Mtb). However, the role of Mtb proteins, particularly those encoded by the genomic regions of deletion (RDs), involved in mediating macrophage ferroptosis has not been thoroughly investigated. This study aimed to screen for Mtb RD region-encoded proteins that induce macrophage ferroptosis and elucidate the underlying molecular mechanisms. - Source: PubMed
Publication date: 2026/05/11
Qu ZiluZhou YuanyuanCai QinzhenChen TianXiang YunChen LiuqingYuan Chunhui - Diabetes-associated cognitive dysfunction (DACD) is a severe neurological complication of type 2 diabetes. Impaired autophagic flux is a critical contributor to the progression of DACD. This study aimed to clarify how tripartite motif-containing 25 (TRIM25) regulates autophagy in DACD. To mimic the hyperglycemic environment of diabetes, HT22 hippocampal neurons were exposed to high glucose (HG). Autophagic flux was monitored using an RFP-GFP-LC3 reporter. Transcriptional regulation was evaluated using chromatin immunoprecipitation and a dual-luciferase reporter assay. Protein stability and ubiquitination were examined using a cycloheximide chase assay and co-immunoprecipitation. Protein abundance was determined by western blot, whereas mRNA levels were quantified by reverse transcription quantitative polymerase chain reaction. In HT22 hippocampal neurons exposed to HG, TRIM25 expression was significantly upregulated, whereas sine oculis homeobox 2 (SIX2) and sprouty-related EVH1 domain-containing protein 2 (SPRED2) expression was significantly downregulated. TRIM25 directly interacted with SIX2 and promoted its ubiquitination and degradation. Moreover, TRIM25 inhibited neuronal autophagy under HG conditions by targeting SIX2. SIX2 transcriptionally activated SPRED2 expression and subsequently inhibited extracellular signal-regulated kinase (ERK) phosphorylation. HG-induced reductions in cell viability and autophagy were reversed by SIX2 overexpression but not when SPRED2 was simultaneously knocked down. TRIM25 reduces SPRED2 transcription by mediating the ubiquitination and degradation of SIX2, thereby exacerbating the suppression of neuronal autophagy under high-glucose conditions. This study identifies a novel TRIM25/SIX2/SPRED2/ERK axis through which hyperglycemia impairs neuronal autophagy. - Source: PubMed
Publication date: 2026/05/09
Chen LiZhou XiankeTan HongBao - TRIM25 is an E3 ubiquitin ligase involved in various cellular processes due to its enzymatic activity. In particular, it plays a role in antiviral innate immunity. Here, we demonstrate that TRIM25 modulates hypoxia signaling. TRIM25 interacts with HIF-1α and HIF-2α, stabilizing them. TRIM25 catalyzes K11-linked polyubiquitination of HIF-1α at K719 and K721 and of HIF-2α at K709. This results in the stabilization of the proteins and enhanced hypoxia signaling. Moreover, TRIM25-mediated augmentation of hypoxia signaling depends on HIF-1α. Trim25-deficient mice are more sensitive to hypoxia, and zebrafish lacking trim25 show a similar phenotype. These data reveal TRIM25's role in regulating hypoxia signaling and provide insight into a new mechanism that modulates the stabilization and activity of HIF-1α and HIF-2α. - Source: PubMed
Publication date: 2026/05/06
Li ZiyiLi JunLi ZhiWang RuiYuan LeSong YananWang YanyiYan RunkunLai FuxiangWang JingXiao Wuhan - Innate immune sensors rely on ubiquitin ligases to calibrate antiviral responses, yet the rules governing substrate recognition by SPRY-containing ligases remain poorly defined. Here, we establish a large-scale structure-based screening pipeline using AlphaFold to systematically predict interactions between human nucleic acid sensors and SPRY-containing proteins. Our approach uncovered novel transient or degradation-sensitive interactions that are typically missed by proteomic methods, including a labile TRIM58-OAS1 complex. We show that SPRY domains dictate substrate specificity: TRIM25 preferentially engages ZAP, whereas Riplet favors RIG-I. Domain-swapping experiments demonstrated that SPRY domains are sufficient to reprogram ligase specificity and antiviral activity. Phylogenetic and structural analyses revealed that TRIM25 and Riplet evolved from a common ancestor but diverged in coiled-coil architecture and oligomeric state, while retaining conserved substrate preferences. Residue-level modeling identified hypervariable SPRY loops as critical determinants of recognition, a prediction validated by targeted mutagenesis of the TRIM25-ZAP interface. Finally, we show that distinct SPRY-containing ligases surveil self-amplifying RNA (saRNA) vaccines: Riplet-RIG-I primarily responds when RNA is delivered by lipofection, whereas TRIM25-ZAP is engaged upon lipid nanoparticle delivery, with functional consequences for vaccine expression. Together, these findings demonstrate that SPRY domains encode recognition logic for ubiquitin ligases, that AlphaFold enables discovery of otherwise hidden interactions and that these principles have direct implications for RNA-based therapeutics. - Source: PubMed
Publication date: 2026/05/08
Syed IbrahimChen ShengPeeler David JMcKay Paul FBriones-Orta Marco ABohn Jennifer AShattock Robin JGonçalves-Carneiro Daniel