RNF126 Pre-design Chimera RNAi
- Known as:
- RNF126 Pre-design Chimera RNAi
- Catalog number:
- H00055658-R02
- Product Quantity:
- 10 nmol
- Category:
- -
- Supplier:
- Abno
- Gene target:
- RNF126 Pre-design Chimera RNAi
Related genes to: RNF126 Pre-design Chimera RNAi
- Gene:
- RNF126 NIH gene
- Name:
- ring finger protein 126
- Previous symbol:
- -
- Synonyms:
- FLJ20552
- Chromosome:
- 19p13.3
- Locus Type:
- gene with protein product
- Date approved:
- 2003-05-21
- Date modifiied:
- 2019-04-16
Related products to: RNF126 Pre-design Chimera RNAi
Related articles to: RNF126 Pre-design Chimera RNAi
- The mechanistic target of rapamycin complex 1 (mTORC1) serves as a central metabolic hub that integrates nutrient signals and orchestrates cellular metabolism to regulate many fundamental cell processes. While mTORC1 activation is known to occur both on lysosomal membranes and at the Golgi apparatus in response to environmental cues, the molecular mechanisms governing its Golgi-associated activation remain poorly understood. In this study, we identified YIF1A as a novel Golgi-localized regulator of growth factor-mediated mTORC1 signaling. Mechanistically, YIF1A interacted with the E3 ubiquitin ligase RNF126 to facilitate K48-linked polyubiquitination of G3BP1/2, thereby promoting mTORC1 activation. Genetic depletion of either YIF1A or RNF126 stabilized G3BP1/2 proteins and significantly impaired mTORC1 activity. Notably, YIF1A knockdown conferred resistance to etoposide- and doxorubicin-induced cellular senescence. The evolutionary conservation of this pathway was demonstrated by extended or shortened lifespan in Caenorhabditis elegans lacking or overexpressing yif-1, the invertebrate ortholog of YIF1A. Our findings not only elucidate a previously unrecognized Golgi-specific regulatory axis for mTORC1 activation but also suggest YIF1A as a potential therapeutic target for modulating aging-related pathologies. - Source: PubMed
Publication date: 2026/06/23
Zhang XiaogangLiu LuyingShang MengdiHu BinZhu ShuWang XiLiu JieyingHan YanchunWei XiaodanCao QiLi FanGao LijieSun JingyuYu JiaqiTan ChentaiDong MenghuaTang Tie-ShanWang Jiu-Qiang - Fetal growth restriction (FGR) remains a major contributor to neonatal morbidity and mortality worldwide, with limited effective diagnostic and therapeutic options. To better understand its molecular mechanism, we performed integrated multi-omics analyses of placental tissues from FGR pregnancies and normal controls, identifying Ring Finger Protein 126 (RNF126), an E3 ubiquitin ligase, as a key regulator of FGR and a potential biomarker distinguishing FGR from small-for-gestational-age (SGA) fetuses. Placenta-specific RNF126 conditional knockout (cKO) mice demonstrated a causal role of elevated placental RNF126 in FGR development . Functional studies revealed that RNF126 induced endoplasmic reticulum (ER) stress and apoptosis in trophoblasts. Mechanistically, RNF126 promoted a ubiquitin-proteasome-mediated degradation of the MYH9/MYH10 complex, thereby exacerbating ER stress and impairing trophoblast function, with lysine 833 (K833) of MYH9 identified as a critical ubiquitination site. Collectively, these findings elucidate an RNF126-mediated pathogenic mechanism in FGR and highlight RNF126 as a promising biomarker and therapeutic target. - Source: PubMed
Publication date: 2026/06/08
Lu LilinYe XiaomeiLan JiawenXu ShuxiuCheng ManyuLv ChenlinZhou JunLi Jing - Myeloid differentiation factor 88 (MyD88) is a critical mediator of inflammatory signaling. However, the development of MyD88 inhibitors has been limited, and there are no reports on MyD88 degraders. Based on our previously identified MyD88 inhibitor and employing a template-assisted modification strategy, we designed and synthesized 40 novel derivatives, and identified the optimal compound , which could inhibit nuclear factor kappa-light-chain-enhancer of activated B cells (NF-κB) pathway activation by facilitating the interaction between ring finger protein 126 (RNF126) (an E3 ubiquitin ligase) and MyD88, thereby promoting ubiquitination and subsequent degradation of MyD88. The subacute toxicity test indicated that had good safety profile. Furthermore, it demonstrated significant anti-inflammatory effects in both cecal ligation and puncture (CLP) and lipopolysaccharide (LPS) induced acute lung injury (ALI) models, effectively ameliorating ALI symptoms. These findings suggest that holds considerable promise as a MyD88-targeting molecular glue degrader for the treatment of ALI. - Source: PubMed
Publication date: 2026/06/12
Zhu LuxiaoTang DanChen TingSun ChenhuiDong KeChen QiDai QinxueMo YunchangChen PanSun JinfengLiang GuangTang Qidong - Tumor hypoxia promotes dedifferentiation and metabolic reprogramming in hepatocellular carcinoma (HCC), undermining normal liver functions. Here, we identify the E3 ubiquitin ligase RNF126 as a hypoxia-inducible "peroxisomal fate" switch that links the hypoxic microenvironment to loss of hepatocyte differentiation. Under hypoxia, HIF-2α drives RNF126 expression, which in turn ubiquitinates the peroxisomal membrane transporter ABCD3, triggering selective peroxisome autophagy (pexophagy) and depletion of peroxisomes. This organelle loss ablates very-long-chain fatty acid β-oxidation and hydrogen peroxide detoxification, erasing key hepatocyte differentiation features. We show that genetic RNF126 ablation restores peroxisomal functions and impairs hypoxic HCC growth. Leveraging these insights, we developed a small-molecule RNF126 inhibitor, D665-1412, which selectively blocks hypoxia-induced pexophagy. D665-1412 treatment stabilizes peroxisomes, normalizes lipid metabolism, and reactivates hepatocytic differentiation markers, thereby "redifferentiating" HCC cells and suppressing tumor progression in vitro and in vivo. Our findings establish the HIF-2α-RNF126-ABCD3 axis as a driver of HCC dedifferentiation and present organelle-targeted redifferentiation therapy as a promising approach for liver cancer. - Source: PubMed
Publication date: 2026/06/09
Su QiYang YichunRen JiayanZhang YuFu LijuanWu QingHan XuZhang Yanmin - Gliomas are highly invasive brain tumors in which metabolic reprogramming plays a pivotal role in tumor initiation and progression. METTL17, a mitochondria-associated methyltransferase, has been reported to enhance oxidative phosphorylation (OXPHOS) through mitochondrial RNA methylation; however, its function and regulatory mechanisms in glioma remain poorly understood. In this study, we manipulated METTL17 expression in primary P1 and U251 glioma cells using lentiviral-mediated knockdown and overexpression approaches. METTL17 depletion significantly suppressed cell proliferation, migration, and invasion, reduced ATP production and mitochondrial membrane potential, and increased reactive oxygen species accumulation, whereas METTL17 overexpression reversed these phenotypes. Mechanistically, METTL17 sustained mitochondrial OXPHOS by positively regulating key components of the electron transport chain, including NDUFA2, NDUFS1, SDHB, UQCRB, and MT-CO2. Mass spectrometry and co-immunoprecipitation analyses further revealed that METTL17 interacts with the E3 ubiquitin ligase RNF126, which destabilizes METTL17 through K116-dependent ubiquitination. Additionally, we demonstrate that SIRT5 acts as a desuccinylase for METTL17, removing succinylation at Lys274 and thereby facilitating RNF126-mediated ubiquitination and degradation of METTL17. In vivo xenograft experiments further validated that METTL17 knockdown markedly inhibited tumor growth and enhanced apoptosis. Collectively, these findings identify METTL17 as a critical regulator of mitochondrial function and energy metabolism in glioma and reveal a SIRT5-METTL17-RNF126 axis that governs METTL17 stability, providing new insights into glioma metabolic reprogramming and potential therapeutic targets. - Source: PubMed
Publication date: 2026/04/22
He ChunyanZhang ZixiaoWu XiaokeLin ChangjieJin JieyuNi YongQian YingfengWang Yin