TRIM10 antibody - C-terminal region (ARP34424_T100)
- Known as:
- TRIM10 (anti-) - C-terminal region (ARP34424_T100)
- Catalog number:
- arp34424_t100
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- TRIM10 antibody - C-terminal region (ARP34424_T100)
Related genes to: TRIM10 antibody - C-terminal region (ARP34424_T100)
- Gene:
- TRIM10 NIH gene
- Name:
- tripartite motif containing 10
- Previous symbol:
- RNF9
- Synonyms:
- RFB30, HERF1
- Chromosome:
- 6p22.1
- Locus Type:
- gene with protein product
- Date approved:
- 1999-06-18
- Date modifiied:
- 2016-10-05
Related products to: TRIM10 antibody - C-terminal region (ARP34424_T100)
Related articles to: TRIM10 antibody - C-terminal region (ARP34424_T100)
- The journal retracts the article "TRIM10 is downregulated in acute myeloid leukemia and plays a tumor suppressive role via regulating NF-κB pathway" [...]. - Source: PubMed
Publication date: 2026/05/08
Li LinLi QiZou ZhengrongHuang ZoufangChen Yijian - ObjectiveGout is a prevalent form of inflammatory arthritis in which many patients respond suboptimally to current therapies. Drug development is hampered by a lack of genetically validated targets, leading to high clinical trial attrition. This study aimed to systematically identify and prioritize novel, druggable targets for gout via a multilayered genetic and functional genomics approach.MethodsWe performed two-sample Mendelian randomization (MR) using cis-expression quantitative trait locus (cis-eQTL) data and dual independent gout genome-wide association study (GWAS) cohorts (openGWAS and FinnGen). The candidate genes were subjected to a rigorous validation pipeline including Bayesian colocalization, phenome-wide association studies (PheWASs) to assess pleiotropy and on-target safety, and single-cell RNA sequencing (scRNA-seq) to delineate the cellular context. Molecular docking was used to evaluate the structural druggability of prioritized targets.ResultsMR analysis revealed 15 genes causally associated with gout. Colocalization analysis (PPH4 > 0.8) prioritized two targets: ZSCAN16 (risk-increasing, OR = 1.04, 95% CI [1.02-1.06]) and TRIM10 (protective, OR = 0.96, 95% CI [0.94-0.98]). Crucially, PheWAS revealed that ZSCAN16 is highly specific to gout, whereas TRIM10 exhibited extensive pleiotropy with hematological and cardiometabolic traits, indicating significant safety risks. Single-cell analysis provided orthogonal validation, demonstrating flare-specific upregulation of ZSCAN16 in cytotoxic T/NK cells. Molecular docking confirmed ZSCAN16 as a structurally druggable target, showing high-affinity binding with known compounds (e.g. digoxin, binding energy = -9.6 kcal/mol).ConclusionsOur study identifies ZSCAN16 as a high-potential, druggable therapeutic target for gout, highlighting its genetic influence on specific immune cell activities during acute flares. Conversely, TRIM10 was deprioritized owing to substantial pleiotropic liabilities and poor chemical tractability. These findings suggest that ZSCAN16 could play a crucial role in the pathogenesis of gout and may provide a valuable lead for future drug discovery efforts. - Source: PubMed
Publication date: 2025/12/10
Chen ChuanliangZheng XifanLi ZemingWang HongtaoYao Jun - Mammalian erythroid cells undergo extensive organelle and protein remodeling during erythropoiesis. The transcriptome and proteome of ubiquitin E3 ligases change dynamically during erythroid differentiation, yet mechanisms beyond E3 activity remain unclear. Here, we identify that tripartite motif-containing protein 10α (TRIM10α), an erythroid- and stage-specific E3 ligase, as crucial for stepwise erythroid maturation. TRIM10α self-association to localize on erythroblast surfaces, binding extracellular complement C1q, which facilitates pyrenocyte encapsulation and macrophage recognition. Surface C1q interacts with EpoR to promote lysosomal degradation, and its depletion prolongs Epo signaling. Notably, cytosolic TRIM10α enhances hemoglobin (Hb) maturation and sequesters Hb aggregates under oxidative conditions. Ultimately, TRIM10α self-ubiquitination and its binding to p62 are anticipated to lead to TRIM10α degradation, promoting the removal of Hb aggregates via autophagy. In contrast to TRIM10α, an alternatively spliced TRIM10β, which is barely expressed in human tissues and cells, forms deleterious aggregates, suggesting that evolutionary suppression of TRIM10β supports erythroid homeostasis. Our findings propose that aberrant TRIM10 expression drives erythroid-related diseases and highlight TRIM10 as a potential biomarker or therapeutic target. - Source: PubMed
Publication date: 2025/10/30
Kim HeesooShin WonjiLee DongeunJeon ByunghoonKim YongboShin DonghyukJeong HyobinHong Jun YoungLee SungwookPark Boyoun - Tripartite motif (TRIM) proteins constitute one of the largest subfamilies of RING-type E3 ubiquitin ligases and are attractive targets for the development of novel degraders that exploit the ubiquitin-proteasome pathway. More than half of all TRIM family members contain a PRYSPRY domain, a potentially druggable protein interaction module, located in their C-terminal region. Here, we have determined crystal structures of the PRYSPRY domains from nine TRIM family proteins: TRIM1 (MID2), TRIM9, TRIM10, TRIM11, TRIM15, TRIM16, TRIM18 (MID1), TRIM36, and TRIM67. These structures reveal conservation of the overall β-sandwich topology, despite low sequence conservation, with a unique subdomain swap observed in TRIM11. Significant variations were found in the loops flanking the canonical substrate-binding site, which modulate the shape and electrostatic properties of the binding pocket, hinting at substantial differences in substrate specificity and binding modes among family members. TRIM36 features a unique structural motif between the canonical β-strands 2 and 3, leading to the formation of a dimer, with the canonical substrate-binding site partially occluded by the dimerization motif. In addition, we mapped the locations of missense mutations in MID1 associated with X-linked Opitz syndrome, suggesting that some of these mutations impair the conformational stability of the protein. Taken together, our data provide intriguing insights into the structural and functional divergence of TRIM family PRYSPRY domains, their potential druggability and substrate recognition, and the challenges of ligand design. - Source: PubMed
Publication date: 2025/07/30
Zhubi RezartChaikuad ApiratMuñoz Sosa Christian JJoerger Andreas CKnapp Stefan - The inflammatory response in liver sinusoidal endothelial cells (LSECs) is crucial to the pathophysiology of postoperative hepatic failure. The unfolded protein response (UPR) in LSECs following surgical stress exerts an important mechanism for resolving endothelial inflammation and re-establishing liver homeostasis. We employed 80% hepatectomy in mice to simulate extended hepatectomy and verified the gene expression in the patients who underwent marginal hepatectomy. The UPR in LSECs and endothelial inflammation were induced with tunicamycin or lipopolysaccharides in HUVECs to investigate the expression, effect, and regulation of activating transcription factor 6 (ATF6) in endothelial inflammation. We found that UPR protein ATF6 in LSECs was upregulated and activated following extended hepatectomy in both mice and humans; ATF6 deficiency in mice by either global knockout or LSECs-specific knockdown failed to alleviate the inflammatory response and led to severe liver injury; genetic knockout or pharmacological inhibition of ATF6 by the ATF6 antagonist Ceapin-A7 in HUVECs led to severe inflammation through the nuclear factor-κB (NF-κB) signaling pathway, while the ATF6 agonist AA147 ameliorated inflammation. Mechanistically, ATF6 induced negative transcriptional control of tripartite motif-containing protein 10 (TRIM10) and the downstream NF-κB signaling pathway, thereby suppressing endothelial inflammation. Taken together, our data identify ATF6 as a suppressor of endothelial inflammation following extended hepatectomy and clarify the underlying regulatory mechanism of the ATF6-TRIM10/NF-κB signaling pathway. These findings highlight its potential as a therapeutic target for postoperative hepatic failure. - Source: PubMed
Shi Cheng-ChengYang Dong-JingBai YangZhou BinhuiSun Yao-HuiXu Xiao-RanGuo Wen-ZhiZhang Shui-JunLiang YinmingJin YangShi Ji-Hua