TRAF6 antibody - middle region (ARP30226_P050)
- Known as:
- TRAF6 (anti-) - middle region (ARP30226_P050)
- Catalog number:
- arp30226_p050
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- TRAF6 antibody - middle region (ARP30226_P050)
Related genes to: TRAF6 antibody - middle region (ARP30226_P050)
- Gene:
- TRAF6 NIH gene
- Name:
- TNF receptor associated factor 6
- Previous symbol:
- -
- Synonyms:
- RNF85
- Chromosome:
- 11p12
- Locus Type:
- gene with protein product
- Date approved:
- 1997-06-12
- Date modifiied:
- 2015-11-20
Related products to: TRAF6 antibody - middle region (ARP30226_P050)
Related articles to: TRAF6 antibody - middle region (ARP30226_P050)
- TRAF6 is traditionally recognized as an antiviral ubiquitin E3 ligase that positively regulates the production of type I interferon and inflammatory cytokines. However, our study reveals that TRAF6 also plays a crucial role in the lytic replication of Kaposi's sarcoma-associated herpesvirus (KSHV). Mechanistically, during KSHV lytic replication, TRAF6 mediates the K63-linked polyubiquitination and activation of Akt, which is required for the efficient viral replication. Disruption of TRAF6 or Akt expression through CRISPR-mediated knockout, or inhibition of TRAF6 or Akt with small molecule inhibitors, reduces KSHV replication efficiency. Conversely, expression of constitutively active Akt can rescue the impaired replication caused by TRAF6 deficiency. Notably, the TRAF6-Akt axis is also required for the lytic replication of Epstein-Barr virus but not for Human cytomegalovirus. These findings highlight the role of the TRAF6-Akt axis in the life cycle of oncogenic herpesviruses and suggest potential therapeutic targets for related diseases. - Source: PubMed
Publication date: 2026/09/01
Liu ZhenshanGuo QingyuWang WeiliLu HongjiaYu TianyuLi TingtingLiang Qiming - Interferon regulatory factors (IRFs) are DNA-binding transcription factors involved in immune regulation, yet the composition and physiological relevance of IRF repertoires in bivalve molluscs remain incompletely understood. In this study, comparative genomic, phylogenetic, structural and transcriptomic analyses were integrated to examine IRF evolution and immune-associated expression in bivalves. IRF genes were identified from representative bivalve proteomes and analyzed together with IRFs from model animals and previously characterized molluscan sequences. The dataset comprised 29 bivalve species from 12 families. Within this sampled dataset, IRF copy number ranged from two to four per species, with most species retaining three members, indicating a restricted IRF repertoire. Phylogenetic analysis of 113 IRF proteins from 34 species resolved four major subfamilies. Bivalve IRFs were mainly assigned to IRF1/2-like and IRF4/8/9-related lineages, whereas in the present dataset, clear bivalve representatives of vertebrate IRF3/7 and IRF5/6 clades were not detected. Motif and gene-structure analyses indicated conservation of the N-terminal IRF DNA-binding region, while the middle and C-terminal regions were more variable, particularly in IRF4/8-like members. In the noble scallop Mimachlamys nobilis, IRF genes and selected IRF-related genes, including MyD88, TRAF6-like, TBK1/IKKε-like and IKKα/β-like candidates, showed gene-specific expression patterns across tissues, with several genes reaching their highest mean expression in the gill, and showed distinct temporal expression profiles over 72 h of Vibrio parahaemolyticus exposure. Re-analysis of oyster and mussel transcriptomes further showed that IRF genes were expressed together with adaptor and kinase genes under bacterial exposure or in gill-associated immune contexts. These findings suggest that bivalves maintain a restricted but immune-relevant IRF repertoire, and that the potential functional diversification of molluscan IRFs is likely shaped by structural divergence, tissue-biased deployment and differential association with upstream innate immune signaling components rather than by extensive gene-family expansion. - Source: PubMed
Publication date: 2026/08/25
Liao WeiminXie ZekunLiu ShitongSu HailongHu HaixinHe QiqiXu TianyiZhang HongkuanZheng Huaiping - AKT (protein kinase B, PKB) coordinates the balance between anabolic and catabolic signaling in skeletal muscle through distinct ubiquitin chain types. Some E3 ubiquitin ligases (E3s) and deubiquitinases (DUBs) form stable binary complexes via non-catalytic interfaces, adding a regulatory layer unavailable to either enzyme alone. This mechanistic synthesis review presents a systematic literature analysis (inception to May 2026; 26 eligible studies). It identified four E3-DUB pairs proposed to regulate AKT in skeletal muscle. These are TRAF6-CYLD (plasma-membrane K63-ubiquitination), MUL1-USP9X (mitochondrial K48-ubiquitination of AKT2), CHIP-UCH37 (proteasome-proximal quality control), and SCF-Skp2-USP37 (PHLPP1/2-dependent control of AKT Ser473 phosphorylation). All four interfaces are structurally separate from the catalytic sites and are regulated by upstream kinase phosphorylation. Evidence for the four pairs is markedly uneven. TRAF6-CYLD is supported by endogenous co-immunoprecipitation and functional data in muscle models. CHIP and UCH37 each act on AKT-related substrates independently and are individually well documented, but a direct CHIP-UCH37 interaction has not itself been demonstrated. SCF-Skp2-USP37 interaction data rest on a real but non-muscle direct interaction, whereas MUL1-USP9X has no reported direct interaction at all; CHIP-UCH37, SCF-Skp2-USP37, and MUL1-USP9X are therefore all presented as testable hypotheses of varying strength. In chronic atrophy, available data are consistent with disruption of these complexes contributing to AKT suppression through parallel, largely independent mechanisms. However, simultaneous disruption of all four has not been demonstrated in a single system. Available gene expression and protein datasets from sarcopenic muscle broadly support these predictions, though direct experimental validation in human tissue remains pending. This complex-centric framework recasts AKT ubiquitination as an integrated regulatory framework. Each structurally autonomous interface may represent a potentially distinct target for muscle-wasting conditions that currently lack approved therapies. - Source: PubMed
Dabur Rajesh - Sepsis-associated liver dysfunction is a life-threatening condition with a high mortality rate and no mechanism-based therapy. In this study, we identify the cross-linking enzyme transglutaminase 2 (TG2) as a driver of liver inflammation by activating macrophages in a mouse model of sepsis. Pharmacological inhibition of TG2 improves survival and reduces multiorgan inflammation, with the liver as a primary therapeutic target. Mechanistically, TG2 activity was up-regulated in macrophages, where it cross-linked vimentin to promote oligomerization and intermediate filament remodeling. Genetic ablation of TG2 or vimentin suppressed macrophage cytokine production and attenuated lipopolysaccharide-induced inflammation. Notably, vimentin-deficient macrophages exhibited enhanced proteasome recruitment to detergent-insoluble protein aggregates, accelerating the degradation of proinflammatory mediators such as Traf6, thereby dampening nuclear factor κB signaling. Proteomic profiling revealed a previously unrecognized Rab27a-positive vesicle trafficking pathway for inflammatory aggregate clearance. Together, these findings define a TG2-vimentin axis that controls macrophage activation through proteostasis regulation, linking cytoskeletal remodeling to inflammatory signaling. - Source: PubMed
Publication date: 2026/08/28
Xu YaliSu TingMishra HrichaDohmae NaoshiSuzuki TakehiroSakamaki YurikoAoyagi HaruyoAizaki HidekiNishimura HajimeFuruhata ErinaGong YuqingCheng QiZhang BeiyuanHe ChenzheYanaka KaoriFurutani YutakaTatsukawa HidekiSuzuki HarukazuYu WenkuiQin Xian-Yang - Tumor necrosis factor receptor-associated factor 6 (TRAF6) is a central E3 ubiquitin ligase that links immune-receptor activation to nondegradative K63-linked ubiquitin signaling. Through its functional cooperation with the E2 enzyme Ubc13/UBE2N and Uev1A, TRAF6 promotes the formation of polyubiquitin scaffolds that activate TAK1, IKK, NF-κB, MAPK, inflammasome-related pathways, and multiple cancer-associated signaling networks. Because excessive or dysregulated TRAF6 activity contributes to chronic inflammation, autoimmune disease, tumor progression, metabolic reprogramming, immune evasion, and therapy resistance, the TRAF6-Ubc13 interface has emerged as an attractive but challenging target for small-molecule intervention. This review summarizes the structural and mechanistic basis of TRAF6-Ubc13-dependent ubiquitin transfer, highlighting the roles of TRAF6 RING-domain dimerization, zinc-finger support, oligomerization, and Ubc13 engagement in productive K63-linked ubiquitination. Particular emphasis is placed on C25-140, the principal validated small-molecule disruptor of the TRAF6-Ubc13 interaction, and on its ability to suppress TRAF6 E3 ligase activity and attenuate inflammatory signaling in cellular and disease models. The review also evaluates related therapeutic strategies, including Ubc13/UBE2N inhibitors, TRAF6-targeted natural products and synthetic modulators, receptor-side TRAF6 protein-protein interaction inhibitors, and emerging approaches aimed at TRAF6 oligomerization or phase-separated signaling complexes. Although current pharmacological evidence remains limited, available data support TRAF6-Ubc13 disruption as a promising strategy for selectively modulating pathological ubiquitin signaling in inflammation and cancer. Future progress will depend on improved ligand-bound structural validation, selective chemical probes, optimized pharmacological properties, and disease-specific biomarker-guided application. - Source: PubMed
Publication date: 2026/08/27
Alkhedhairi Saleh