Ask about this productRelated genes to: TRIM27 antibody
- Gene:
- TRIM27 NIH gene
- Name:
- tripartite motif containing 27
- Previous symbol:
- RFP
- Synonyms:
- RNF76
- Chromosome:
- 6p22.1
- Locus Type:
- gene with protein product
- Date approved:
- 1995-05-09
- Date modifiied:
- 2016-10-05
Related products to: TRIM27 antibody
Related articles to: TRIM27 antibody
- The WASH complex regulates endosomal trafficking and is linked to several neurodevelopmental diseases, including Prader-Willi syndrome, Schaaf-Yang syndrome, and Hao-Fountain syndrome. Its function is tightly controlled by ubiquitination, maintained by the multi-subunit MUST complex containing both a ubiquitin ligase (MAGEL2/TRIM27) and a deubiquitinase (USP7). However, the mechanism underlying the MUST complex assembly remains poorly understood. In this study, we investigate the assembly of USP7 and MAGEL2 components of the MUST complex using NMR spectroscopy, isothermal titration calorimetry, X-ray crystallography, and cellular assays. We show that the USP7/MAGEL2 interaction is bipartite and multivalent. Two distinct domains of USP7, TRAF and UBL1-2, recognize two unstructured but evolutionarily conserved regions of MAGEL2, one of which contains multiple TRAF-binding sites. Furthermore, we determine the high-resolution crystal structure of the TRAF/MAGEL2 complex and identify Hao-Fountain syndrome-linked mutations in USP7 that disrupt USP7/MAGEL2 complex formation and in cells. These findings provide mechanistic insight into the pathogenic basis of Hao-Fountain syndrome and related Schaaf-Yang and Prader-Willi syndromes. - Source: PubMed
Publication date: 2026/04/28
Korchak Emilie JSoriano Gabriella ASemenova IrinaHao BingŠtepihar DenisBayat TaraFon Tacer KlementinaBezsonova Irina - Hepatocellular carcinoma (HCC) is characterized by a highly immunosuppressive microenvironment, which contributes to its unfavorable clinical outcomes. Myeloid-derived suppressor cells (MDSCs) play a crucial role in this process. Schisandrin B (SchB) shows anti-tumor potential, but its mechanism in suppressing MDSCs remains unclear. This study investigates how SchB inhibits MDSCs accumulation and enhances anti-PD-1 therapy efficacy in HCC.SchB's efficacy and mechanism were investigated both in vitro and in vivo. In vitro, MTT, wound healing, EdU, colony formation, flow cytometry, ELISA, western blot, immunofluorescence, Co-IP, molecular dynamics (MD), and CETSA assays were employed to evaluate the therapeutic effects and mechanistic action of SchB on HCC. In vivo, a mouse HCC xenograft model was used to evaluate whether SchB could enhance the anti-tumor effect of PD-1 mAb and the potential mechanism.Mechanistically, SchB suppressed TRIM27 expression, disrupted the interaction between TRIM27 and STING, and enhanced STING/TBK1/IRF3 signaling, thereby suppressing the secretion of IL-6 and GM-CSF as well as the accumulation of MDSCs. SchB could directly bind to TRIM27 and downregulate its expression, thereby enhancing STING protein stability. In vivo, SchB effectively reduced MDSCs accumulation while promoting T cell recruitment, thereby augmenting the antitumor efficacy of PD-1 mAb therapy.SchB up-regulates STING by suppressing TRIM27, inhibits IL-6/GM-CSF secretion, and reduces MDSCs accumulation, indicating that SchB has the potential to be a promising candidate for PD-1 inhibitor therapy in HCC. - Source: PubMed
Publication date: 2026/05/05
Huang LeiLi SiyingLi ZiqingQin ZhuoSun YananQin CaifangWang ChunmeiLi HeSun JinghuiWu JipingZhang Zhihong - The E3 ubiquitin ligase tripartite motif 27 (TRIM27) is a negative regulator of NF-κB activation and the innate immune response, and TRIM27 deficiency significantly impairs dextran sulfate sodium (DSS)-induced colitis. The function of TRIM27 in intestinal epithelial cells (IECs), the mechanism by which TRIM27 inhibits the NF-κB pathway and its dysregulation in ulcerative colitis (UC) remain unclear. Here, it is report that epithelial TRIM27 functions as an anti-inflammatory factor that inhibited intestinal inflammation in IECs in vitro and in epithelial Trim27 knockout mice in vivo. Mechanistically, TRIM27 destabilized IKKα and TRAF6 via polyubiquitination of IKKα at the K569 site and TRAF6 at the K489 site. In response to TNF-α, IKKβ phosphorylated TRIM27 at S173 to decrease TRIM27 expression by impairing its binding to ubiquitin-specific protease 7 (USP7) and USP7-mediated TRIM27 deubiquitination. Notably, overexpression of TRIM27 enhanced the anti-inflammatory effect of infliximab (IFX) in IECs. TRIM27 is downregulated in inflamed colons from UC patients and is associated with the therapeutic effect of IFX. Overall, this study identifies epithelial TRIM27 as a bona fide negative modulator of intestinal inflammation and USP7/TRIM27-IKK as a new double negative feedback mechanism of the NF-κB pathway, which supports the use of TRIM27 replenishment as a potential therapeutic strategy for UC. - Source: PubMed
Publication date: 2026/04/22
Xu WeiminHua ZhebinDai ZhujiangZhang ShashaJiang YihanGe WensongChen YingWeiWang ZhongchuanZhang BingLiu Chen-YingDu Peng - Idiopathic pulmonary fibrosis (IPF) is a complex disease without clear etiology or effective therapy. While DNA methylation has been implicated in IPF pathogenesis, the tissue-specific causal effects of the epigenetic factors on IPF remain undetermined. Here, we perform epigenome-wide Mendelian randomization using blood-based methylation quantitative trait loci of 420,509 CpG sites and genome-wide association study for IPF to elucidate the causal effects of the CpG sites on IPF. Totally, 452 CpG sites has shown putative causal effects on IPF risk after Bonferroni correction. Among them, 13 CpG sites have shown strong colocalization evidence with genetic factors associated with IPF. Specifically, DNA methylation at CpG sites within MAN2A2 and TRIM27 shows significant differences between IPF lungs and controls, correlating with altered mRNA expressions of these genes in lung tissues. The CpG site in MAN2A2 is a binding site of ZNF384 according to transcription factor databases. RNA sequencing in the TGFβ1-induced alveolar epithelia confirms significantly reduced expression of MAN2A2 and ZNF384 comparing to the controls. Collectively, our study suggests a putative causal link between DNA methylation within MAN2A2 and IPF risk, wherein lung-specific DNA methylation in MAN2A2 may perturb the interaction between ZNF384 and MAN2A2, revealing novel roles for these genes in IPF pathogenesis. - Source: PubMed
Publication date: 2026/04/11
Li ZhaoqiHong LunaLv XingyuYang ShuangyuYe FengzhanHuang LinjieJiang ShanpingZhao Huiying - Microglial activation and dysfunction play pivotal roles in the pathogenesis of ischemic stroke, yet the molecular mechanisms governing their phenotypic plasticity and protective functions remain incompletely understood. Here, we integrated transcriptomic profiling with functional validation to identify TRIM27 as a novel regulator of microglial autophagy and polarization following cerebral ischemia-reperfusion injury. RNA sequencing of CD11b microglia isolated from mice subjected to middle cerebral artery occlusion (MCAO) revealed significant downregulation of Trim27, which was associated with impaired autophagy pathways. In vivo overexpression of TRIM27 via AAV9 delivery markedly attenuated infarct volume, neuronal degeneration, and apoptosis after MCAO. This neuroprotection was accompanied by a shift in microglial phenotype from pro-inflammatory M1 toward anti-inflammatory M2 states, along with enhanced autophagic flux. In vitro, TRIM27 overexpression in oxygen-glucose deprivation/reoxygenation (OGD/R)-treated microglia suppressed mitochondrial reactive oxygen species production and lipid peroxidation, improving cell survival. Mechanistically, TRIM27 physically interacted with and stabilized TANK-binding kinase 1 (TBK1) by inhibiting its ubiquitin-mediated degradation. Notably, genetic ablation of Tbk1 abolished the beneficial effects of TRIM27 on microglial polarization, autophagy, oxidative stress, and neuroprotection both in vivo and in vitro. Our findings establish a TRIM27-TBK1 axis as a critical modulator of microglial function in ischemic stroke, highlighting its potential as a therapeutic target for promoting brain repair through autophagy-dependent immunomodulation. - Source: PubMed
Publication date: 2026/04/09
Xie DujieHu ShunbingLong PanyaoHuang JuanLi XiaoboYuan YiLiu HuaizhengChen Yiwei