Ask about this productRelated genes to: TRIM67 antibody
- Gene:
- TRIM67 NIH gene
- Name:
- tripartite motif containing 67
- Previous symbol:
- -
- Synonyms:
- TNL
- Chromosome:
- 1q42.2
- Locus Type:
- gene with protein product
- Date approved:
- 2004-11-19
- Date modifiied:
- 2014-11-19
Related products to: TRIM67 antibody
Related articles to: TRIM67 antibody
- NFS1 cysteine desulfurase (NFS1) a critical enzyme in iron‑sulfur (Fe-S) cluster biogenesis and mitochondrial iron homeostasis, plays a pivotal role in the dysregulation of iron metabolism, a recognized hallmark of cancer. However, the specific role and regulatory mechanisms of NFS1 in colorectal cancer (CRC) remain poorly understood. This study aimed to elucidate the function of NFS1 in CRC and to uncover the upstream molecular pathways governing its expression. - Source: PubMed
Publication date: 2026/04/30
Wang BingHuang XiaofangXing YulongJiao WeiJiang JianhuaLiu GangLi GuochaoLi QinquanYang ChunyuShi Lianghui - Ischemic stroke is a devastating condition with limited treatment options, where neuroinflammation plays a pivotal role in secondary brain injury. Neural cell adhesion molecule 1 (NCAM1) is implicated in neural development and plasticity, but its specific role in microglia during ischemic stroke remains unclear. Here, we demonstrate that microglial NCAM1 expression is significantly downregulated in the acute phase of ischemic stroke in both human patients and a mouse transient middle cerebral artery occlusion (tMCAO) model. Using microglia/macrophage-specific NCAM1-overexpressing mice, we show that NCAM1 overexpression reduces infarct volume, improves neurological deficits, and enhances long-term functional recovery. Mechanistically, NCAM1 directly interacts with the E3 ubiquitin ligase TRIM67 via its cytoplasmic domain. This NCAM1-TRIM67 complex enhances K63-linked ubiquitination while suppressing K48-linked ubiquitination of IκBα, thereby stabilizing IκBα protein, preventing NF-κB p65 nuclear translocation, and ultimately inhibiting NF-κB-driven neuroinflammation and apoptosis. Furthermore, through molecular docking and high-throughput screening, we identified DB07993 as a potent NCAM1 agonist. DB07993 treatment mimicked the neuroprotective effects of NCAM1 overexpression in vitro and in vivo, primarily through activation of the NCAM1-TRIM67-IκBα axis. Our study unveils a novel regulatory mechanism where microglial NCAM1 serves as a critical brake on post-stroke neuroinflammation and identifies DB07993 as a promising lead compound for developing NCAM1-targeted stroke therapies. - Source: PubMed
Publication date: 2026/03/14
Yu ZongdongYu LuliLu WeiChen PengYan HuanJiang Yong'an - Cerebral infarction is one of the most common ischemic cerebrovascular diseases that can lead to neurological deficits. Remimazolam (RE) is a sedative agent that has been shown to improve neurological disorders. However, the underlying molecular mechanism of RE for the treatment of cerebral infarction remains to be further explored. Oxygen-glucose deprivation/reperfusion (OGD/R) cell model and middle cerebral artery occlusion (MCAO) rat model were constructed. Cell proliferation, apoptosis, and inflammation were evaluated using CCK8 assay, EdU assay, flow cytometry, and ELISA. Ferroptosis-related markers were assessed by commercial kits. The expression of Acyl-CoA synthetase long-chain family member 4 (ACSL4) and tripartite motif-containing 67 (TRIM67) was examined by qRT-PCR or western blot. The interaction between TRIM67 and ACSL4 was confirmed by Co-IP assay. Cerebral injury in MCAO rat model was assessed by histological staining and neurological score. RE treatment enhanced proliferation, repressed apoptosis, inflammation and ferroptosis in OGD/R-induced SK-N-SH cells. RE decreased ACSL4 protein expression, and ACSL4 overexpression could reverse the anti-apoptosis, anti-inflammation and anti-ferroptosis roles of RE in OGD/R-induced SK-N-SH cells. TRIM67 reduced ACSL4 expression by increasing its ubiquitination and degradation. TRIM67 alleviated OGD/R-induced neuronal injury by downregulating ACSL4. RE enhanced TRIM67 protein expression, and TRIM67 knockdown also reversed the neuroprotective effect of RE. Also, RE relieved cerebral injury in the MCAO rat model via promoting TRIM67 expression to repress ACSL4. RE alleviated OGD/R-induced apoptosis, inflammation and ferroptosis through promoting TRIM67-mediated degradation of ACSL4, which provided a possible path for additional research in the therapies of cerebral infarction. - Source: PubMed
Xiao GaopengZhang YongqinYang JiHe JigangZhang YouwuQin WenYu LiuqiongWang LingLi YujinBai Yuncheng - Glioblastoma (GBM) is one of the deadliest malignant tumors in the central nervous system. Temozolomide (TMZ) resistance is a crucial cause of treatment failure in GBM. We intended to explore the molecular mechanisms by which ARSD modulated TMZ resistance in GBM. This study revealed that ARSD was up-regulated in GBM and associated with GBM recurrence and poor prognosis. Furthermore, knockdown of ARSD suppressed glycolysis and increased TMZ sensitivity in GBM cells. Mechanistic insights demonstrated that TRIM67 promoted the ubiquitinated degradation of ARSD through the RING structural domain. Concurrently, overexpression of TRIM67 repressed GBM cell glycolysis and increased sensitivity to TMZ by decreasing ARSD expression. Additionally, TRIM67 down-regulated ARSD to hinder β-catenin-mediated glycolysis in GBM cells and suppressed tumor growth in nude mice. Taken together, TRIM67 suppresses ARSD expression by facilitating its ubiquitin-mediated degradation, thereby inactivating the β-catenin pathway to repress GBM glycolysis and TMZ resistance. This study reveals the TRIM67/ARSD/β-catenin axis as a key regulator of GBM metabolic reprogramming and TMZ resistance, offering a novel therapeutic target. - Source: PubMed
Li XuzhaoGuo FangzhouXu LixinPiao Haozhe - Neuronal morphogenesis depends on extracellular guidance cues accurately instructing intracellular cytoskeletal remodeling. Here, we describe a novel role of the actin binding protein coronin 1A (Coro1A) in neuronal morphogenesis, where it mediates responses to the axon guidance cue netrin-1. We found that Coro1A localizes to growth cones and filopodial structures and is required for netrin-dependent axon turning, branching, and corpus callosum development. We previously discovered that Coro1A interacts with TRIM67, a brain-enriched E3 ubiquitin ligase that binds the netrin receptor DCC, and is also required for netrin-mediated neuronal morphogenesis. Loss of Coro1A and loss of TRIM67 shared similar phenotypes, suggesting that they may function together in the same netrin pathway. A Coro1A mutant deficient in binding TRIM67 was unable to rescue loss of Coro1A phenotypes, indicating that the interaction between Coro1A and TRIM67 is required for netrin responses. Together, our findings reveal that Coro1A is required for proper neuronal morphogenesis, where it collaborates with TRIM67 downstream of netrin. - Source: PubMed
Publication date: 2025/10/14
Ho Chris TEvans Elliot BLukasik KimberlyO'Shaughnessy Ellen CShah AneriHsu Chih-HsuanTemple BrendaBear James EGupton Stephanie L