TRIM25 Antibody
- Known as:
- TRIM25 Antibody
- Catalog number:
- HOM-4317
- Product Quantity:
- 0.1 mg
- Category:
- -
- Supplier:
- Zyagen
- Gene target:
- TRIM25 Antibody
Related genes to: TRIM25 Antibody
- 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 Antibody
Related articles to: TRIM25 Antibody
- Among the intracellular sensors of innate immunity against infection, RIG-I-like receptors (RLRs) serve as cytosolic surveillance sensors that detect viral RNA species. However, the role of kinases in modulating RIG-I in a catalytically-independent manner is not well known. In this study, we report that protein kinase DYRK1B is a novel positive regulator of RIG-I-mediated antiviral innate immunity. Overexpression of DYRK1B markedly amplified RNA virus-induced IFN-I production, whereas CRISPR-mediated knockout of DYRK1B substantially attenuated these antiviral responses. Mechanistic investigation revealed that this regulatory role operates independently of DYRK1B's catalytic kinase function; instead, DYRK1B functions as an adaptor protein that connects TRIM25 with RIG-I, thereby promoting TRIM25-mediated K63-linked polyubiquitination of RIG-I, an essential modification required for RIG-I functional activation. Collectively, our findings reveal that DYRK1B enhances innate immunity against RNA viruses by strengthening the physical association of RIG-I with TRIM25, providing a more profound understanding of the mechanisms involved in antiviral immune regulation. - Source: PubMed
Publication date: 2026/08/10
Zeng XianhuangXie JiaYousaf TanzeelNaz WajeehaNing JieZhang ZelinXu YueWu Chao - Mitochondrial dysfunction and abnormal energy metabolism are important pathological features of Alzheimer's disease (AD). This study investigates how mitochondrial protease YME1L1 affects mitochondrial function and its upstream regulation in the pathogenesis of AD. The AD model was established by using APP/PS1 transgenic mice, primary neurons treated with Aβ1-42, and HT22 cells. The silencing of YME1L1 was achieved to evaluate its effects on mitochondrial function and OPA1 protein hydrolysis. RIP-qPCR and RNA pull-down test were used to evaluate the interaction between HNRNPC and YME1L1 mRNA. The protein succinylation level was detected by proteomic analysis of succinylation, and co-immunoprecipitation (Co-IP) was used to verify the succinylation of HNRNPC. Cognitive ability was tested by behavioral tests, including the Morris water maze, Y-maze, object recognition test, and olfactory test. Finally, the therapeutic potential of SIRT5 was studied by an overexpression experiment in an AD model. YME1L1 was significantly upregulated in the AD model, which promoted mitochondrial dysfunction and neuronal damage through OPA1 hydrolysis. HNRNPC enhances the stability of YME1L1 mRNA through an m6A-dependent mechanism, while its own K50 succinylation enhances the stability of HNRNPC by competitively inhibiting TRIM25-mediated ubiquitination, further amplifying the expression of YME1L1. SIRT5 downregulation in AD elevated HNRNPC succinylation levels. SIRT5 overexpression promoted HNRNPC desuccinylation, reduced YME1L1 expression, restored mitochondrial function, and ameliorated Aβ deposition and cognitive deficits in AD mice. The SIRT5-HNRNPC-YME1L1 axis contributes to AD pathogenesis by disrupting OPA1 proteolysis and mitochondrial dynamics. Targeting HNRNPC succinylation represents a promising therapeutic strategy for AD. - Source: PubMed
Li XueweiYang FanJiang YuyanZhao FeiLiu Fan - Immunotherapeutic strategies for triple-negative breast cancer (TNBC) have yielded only modest response rates, severely limiting patients' clinical outcomes. Clarifying the underlying mechanisms to reverse immunotherapy resistance therefore represents a critical unmet need. In this study, we employed the single-cell RNA sequencing (scRNA-Seq) analysis of human TNBC tissues to identify inositol-trisphosphate 3-kinase B (ITPKB) as a central regulator governing cytotoxic T lymphocyte trafficking into the tumor microenvironment (TME). Ectopic expression of ITPKB robustly enhanced the secretion of C-X-C motif chemokine ligand 9 (CXCL9), a critical chemokine required for effective anti-tumor immune responses. Mechanistically, elevated ITPKB activity accelerated the conversion of inositol 1,4,5-trisphosphate (IP3) to inositol 1,3,4,5-tetrakisphosphate (IP4), thereby dampening IP3-driven endoplasmic reticulum (ER) calcium release. Attenuated intracellular calcium ions (Ca) flux, in turn, promoted the recruitment of signal transducer and activator of transcription 1 (STAT1) and nuclear factor-kappa B (NF-κB) to CXCL9 promoter, driving robust CXCL9 transcription. In addition, utilizing a stepwise virtual screening strategy of 3677 compounds, we identified amentoflavone (AMF) as a novel ITPKB agonist-like compound. AMF treatment could stabilize ITPKB by preventing Trim25-mediated K48-linked ubiquitination and degradation. Notably, in 4T1 and EMT6 syngeneic TNBC murine models, ITPKB-overexpressing or AMF administration exhibited markedly enhanced sensitivity to anti-programmed cell death protein 1 (αPD-1) immune checkpoint blockade. Collectively, these results position ITPKB as a therapeutically tractable molecular switch that remodels the tumor immune landscape via Ca-dependent transcriptional rewiring. Targeting ITPKB thus represents a promising strategy to overcome immunotherapy resistance and expand the pool of TNBC patients who may benefit from αPD-1-based immunotherapy. - Source: PubMed
Publication date: 2026/08/02
Zhang KejingWang XiaYi QiaoliGuan HuajieWang JiayuTan FengyuZhou ZhiyangZhu XudongZhan ChengWang JinWu JianminTang HailinXu ZhijieShuang ZeyuYan Yuanliang - Mammalian embryonic stem cells (ESCs), despite lacking functional interferon (IFN) signaling, are remarkably resistant to viral infection. However, the mechanistic basis of their antiviral defenses remains incompletely characterized. In this study, we investigated the antiviral functional role and molecular mechanism of tripartite motif-containing protein 25 (TRIM25), a well-known key driver of IFN-dependent innate immunity, in IFN-deficient mouse ESCs (mESCs). TRIM25 exhibited a broad spectrum of antiviral activity in mESCs. RNAi depletion or CRISPR-mediated knockout of TRIM25 markedly enhanced the replication and propagation of both encephalomyocarditis virus (EMCV) and vesicular stomatitis virus (VSV) viruses. Mechanistically, the antiviral activity of TRIM25 in mESCs is independent of both IFN production and constitutive ISG expression. In virus-infected mESCs, TRIM25 translocated from the nucleus to the cytoplasm and directly bound viral RNA, where it formed cytoplasmic condensates with GTPase-activating protein-binding protein 1 (G3BP1) that colocalized with dsRNA foci. Genetic perturbation of G3BP1 similarly compromised the antiviral defenses of mESCs, revealing an essential synergism between TRIM25 and stress granule components in restricting viral replication. Our study identifies TRIM25 as a pivotal RNA-sensing effector in ESCs, delineating a previously unrecognized IFN-independent axis of intrinsic immunity that bridges viral RNA surveillance with stress granule-mediated suppression, thereby expanding the paradigm of pluripotent cell-autonomous antiviral strategies. - Source: PubMed
Publication date: 2026/07/30
Zou JieLin YuxinWu ChunyanJi YaoZhao XuankaiXu ZhanGong JingfeiShi ZhiyuanLuo TianyangXie XiaolingJiang YananTian QiZhang ShuqiJi YanxiLi YuanHe ZhenyuZhang ShuchunCao LiuLi Chun-MeiWu JunyuGuo Deyin - Breast cancer (BC) is a highly heterogeneous malignancy, and current treatments often suffer from toxicity, limited selectivity, and high cost. This study aimed to integrate transcriptome-level data, multi-layered network analysis, and drug repositioning strategies to identify candidate diagnostic and prognostic biomarkers for BC and propose potential repositioned drug candidates. - Source: PubMed
Publication date: 2026/07/24
Aydin BusraOkutan Beyza NurSara Fatmanur ElifGulseren GulcihanSinha Raghu