Ask about this productRelated genes to: TRIM23 Blocking Peptide
- Gene:
- TRIM23 NIH gene
- Name:
- tripartite motif containing 23
- Previous symbol:
- ARFD1
- Synonyms:
- ARD1, RNF46
- Chromosome:
- 5q12.3
- Locus Type:
- gene with protein product
- Date approved:
- 1994-06-23
- Date modifiied:
- 2015-08-26
Related products to: TRIM23 Blocking Peptide
Related articles to: TRIM23 Blocking Peptide
- This study aimed to clone and identify the TRIM23 gene (designated as PcTRIM23) from Procambarus clarkii and investigate its immune function during white spot syndrome virus (WSSV) infection. The open reading frame (ORF) of PcTRIM23 was 1719 bp in length, encoding a 572-amino acid protein that contains a RING finger domain, two B-Box domains, a B-Box C-terminal domain (BBC) at the N-terminus and an ADP-ribosylation factor (ARF) domain at the C-terminus. PcTRIM23 exhibited the highest expression levels in the hepatopancreas and gills of P. clarkii, and its expression was significantly upregulated at 6-24 h following WSSV infection. After knocking down PcTRIM23 expression via RNA interference (RNAi), the copy number of WSSV and the transcriptional level of VP28 were markedly increased, showing a correlation between reduced PcTRIM23 expression and enhanced viral replication. Further studies revealed that PcTRIM23 knockdown induced hepatopancreatic cell apoptosis, as evidenced by the increased number of TUNEL-positive cells, mitochondrial vacuolization, the up-regulation of apoptosis-related genes including Cytochrome C (Cyt-C) and caspase-3, and the down-regulation of B-cell lymphoma/leukemia 2 (Bcl-2). In addition, PcTRIM23 knockdown led to the accumulation of reactive oxygen species (ROS) and the decreased expression of antioxidant-related genes such as Nrf2, Cu/Zn-SOD and CAT. In conclusion, our results suggest that PcTRIM23 is associated with a protective role against WSSV infection in P. clarkii, correlating with reduced cell apoptosis and enhanced antioxidant response. However, further rescue experiments are needed to establish a direct causal relationship. This study provides the first functional characterization of crayfish TRIM23 in antiviral immunity and lays a foundation for further investigation of its causal regulatory mechanisms. - Source: PubMed
Publication date: 2026/07/02
Peng ChaoShao LiyeWang RonghuaHuang HaihongChen Zhongyuan - - Source: PubMed
Publication date: 2025/07/03
Acharya DhirajSayyad ZuberwasimHoenigsperger HeleneHirschenberger MaximilianZurenski MatthewBalakrishnan KannanZhu JunjiGableske SebastianKato JiroZhang Shen-YingCasanova Jean-LaurentMoss JoelSparrer Konstantin M JGack Michaela U - Hepatocellular carcinoma (HCC) ranks among the most prevalent malignant tumors worldwide, characterized by high mortality rates. TRIM23, an E3 ubiquitin ligase, represents a potential molecular target for anticancer drug development. Additionally, Hexahydrocurcumin (HHC) exhibits notable anticancer activity as a natural product. Here, we aimed to investigate HHC's anti-tumor role in HCC. Molecular docking assays and Cellular thermal shift assays were employed to predict HHC's potential targeting of TRIM23. Immunofluorescence and western blot analyses were conducted to assess HHC's inhibition of TRIM23 expression. Wound-healing, clone formation, and transwell assays were used to evaluate its anti-tumor efficacy. Quantitative proteome analysis and co-immunoprecipitation (Co-IP) were employed to explore and verify HHC's potential mechanism in HCC cells. Subcutaneous HCC tumor-bearing mice were used to further validate HHC's function in vivo. Public databases confirmed TRIM23 as a potential biomarker of HCC, associated with poor prognosis. Molecular docking and Cellular thermal shift assays confirmed HHC as a direct inhibitor of TRIM23. Subsequent in vitro assays demonstrated HHC's ability to impede HCC cell function. Quantitative proteome analysis revealed upregulation of MBNL1, a tumor suppressor, in HHC-treated HCC cells. Rescue analysis further demonstrated MBNL1 as a substrate of TRIM23, directly influencing the phenotypic outcomes of HHC-treated cells. Additionally, subcutaneous HCC tumor-bearing mice confirmed HHC's efficacy in vivo. Our findings underscore TRIM23 as a promising therapeutic target for HCC treatment, with HHC emerging as an effective therapeutic agent by targeting the TRIM23/MBNL1 axis. - Source: PubMed
Publication date: 2025/07/02
Wang MiWeng ChunyanXu JingliXu Ka - The cGAS-STING pathway, well-known to elicit interferon (IFN) responses, is also a key inducer of autophagy upon virus infection or other stimuli. Whereas the mediators for cGAS-induced IFN responses are well characterized, much less is known about how cGAS elicits autophagy. Here, we report that TRIM23, a unique TRIM protein harboring both ubiquitin E3 ligase and GTPase activity, is crucial for cGAS-STING-dependent antiviral autophagy. Genetic ablation of TRIM23 impairs autophagic control of HSV-1 infection. HSV-1 infection or cGAS-STING stimulation induces TBK1-mediated TRIM23 phosphorylation at S39, which triggers TRIM23 autoubiquitination and GTPase activity and ultimately elicits autophagy. Fibroblasts from a patient with herpes simplex encephalitis heterozygous for a dominant-negative, kinase-inactivating TBK1 mutation fail to activate autophagy by TRIM23 and cGAS-STING. Our results thus identify the cGAS-STING-TBK1-TRIM23 axis as a key autophagy defense pathway and may stimulate new therapeutic interventions for viral or inflammatory diseases. - Source: PubMed
Publication date: 2025/05/13
Acharya DhirajSayyad ZuberwasimHoenigsperger HeleneHirschenberger MaximilianZurenski MatthewBalakrishnan KannanZhu JunjiGableske SebastianKato JiroZhang Shen-YingCasanova Jean-LaurentMoss JoelSparrer Konstantin M JGack Michaela U - Mink enteritis virus (MEV) is an important pathogen causing mink viral enteritis. The mechanisms of cell cycle arrest induced by MEV infection and the roles of autophagy in MEV replication remain unclear. In this study, the roles of MEV NS1 protein in inducing cell cycle arrest were investigated, using the in vitro CRFK cell models. As a result, MEV infection increased the proportion of the cells in S phase, inducing S phase arrest. MEV NS1 protein also led to cycle arrest in S phase. And the deletions of NLS and TAD significantly weakened the ability of NS1 protein to cause cycle arrest in S phase, and NLS and TAD were the indispensable domains of NS1 protein. Furthermore, proteome profiling of the cells infected with MEV at the early stage demonstrated that the autophagy-related protein TRIM23 was significantly up-regulated during MEV infection. To investigate the effects of TRIM23 on MEV replication, the cell models were established, using siRNAs targeting TRIM23. The knockdown of TRIM23 resulted in the decreases in the levels of TBK1 protein and the phosphorylated p62 protein, and an increase in the level of p62 protein in the cells infected with MEV, indirectly influencing virus replication. The findings implied that S phase arrest and the up-regulated TRIM23 induced by MEV infection played the important roles in MEV replication. - Source: PubMed
Publication date: 2025/01/06
Lu-Jiao DongZhi-Juan LiYing-Li SunHua FanWen-Qian LiHui-Ning ZhangJun PengZhi-Jing Xie