Ask about this productRelated genes to: EIF4H Blocking Peptide
- Gene:
- EIF4H NIH gene
- Name:
- eukaryotic translation initiation factor 4H
- Previous symbol:
- WBSCR1
- Synonyms:
- WSCR1, KIAA0038
- Chromosome:
- 7q11.23
- Locus Type:
- gene with protein product
- Date approved:
- 1997-09-12
- Date modifiied:
- 2014-11-19
Related products to: EIF4H Blocking Peptide
Related articles to: EIF4H Blocking Peptide
- Interferon regulatory factor 2 binding protein 2 (IRF2BP2) suppresses the interferon response and inflammation. Individuals who carry 2 copies of a genetic variant (rs3045215) that deletes 9 nucleotides from the long 3'UTR of IRF2BP2 have lower IRF2BP2 protein expression in white blood cells and increased risk of coronary atherosclerosis and calcification. - Source: PubMed
Publication date: 2026/05/28
Duong AnChen Hsiao-HueiStewart Alexandre F R - Williams syndrome (WS; OMIM #194,050) is a multisystem pediatric genetic disorder caused by a heterozygous microdeletion of a 1.5-1.8 Mb region at chromosome 7q11.23, encompassing 26 to 28 genes. Clinical hallmarks include cardiovascular anomalies, distinctive craniofacial morphology and neurodevelopmental deficits characterized by hypersociability, cognitive impairment and anxiety. Although causative therapies for WS still remain elusive, advances in gene editing and forebrain organoids have already greatly furthered our understanding of the underlying mechanisms. - Source: PubMed
Publication date: 2026/03/17
Chen Ya-YueChen Wei-JunZhang RuiJi ChaiZhang Yu-HanMa Da-QingShi Qiao-JuanXie Yi-Cheng - Hepatitis E virus (HEV) is a leading cause of acute viral hepatitis worldwide, responsible for approximately 20 million infections annually. Despite the availability of a vaccine in China, no direct-acting antivirals are approved, and host factors required for HEV replication remain poorly defined. Here, using a genome-wide CRISPR/Cas9 knockout screen in a replicon system, we identified Eukaryotic Translation Initiation Factor 4H (EIF4H) and Y-Box Binding Protein 1 (YBX1) as essential host factors for HEV replication and pathogenesis. Knockout of either factor markedly impaired replication of HEV genotypes 1, 3, and 4, as well as HEV infection and production in hepatocellular carcinoma cells and human induced pluripotent stem cell-derived hepatocyte-like cells, while leaving SARS-CoV-2, hepatitis B virus, hepatitis C virus, and Zika virus unaffected, underscoring their HEV-specific roles. Mechanistically, EIF4H interacts with ORF1 via its methyltransferase-Y-papain-like protease region, and EIF4H deficiency alters the composition of the ORF1-associated replication complex. By contrast, YBX1 is dispensable for ORF1 translation and RNA binding but is specifically required for ORF1 proteolytic processing, a prerequisite for assembling a functional replication machinery. EIF4H knockout rats and liver-specific YBX1 knockout rats were largely resistant to rat HEV-C1 infection, showing profound reductions in viral shedding, suppressed hepatic and intestinal viral loads, and protection from liver pathology. Together, our findings establish EIF4H and YBX1 as essential host factors for HEV infection and pathogenesis and reveal potential targets for antiviral intervention. - Source: PubMed
Publication date: 2026/03/04
Ju XiaohuiDong LinLiu TianxuZhang FanSun XuegeSchwoerer Michael PRen WenlinGong MingliPloss AlexanderQin WeiWu XianfangWang LinDing Qiang - To search for genetic sources of allele-specific mRNA translation, we leveraged heterozygous polymorphisms and variants present in the exome of HCT116 colorectal adenocarcinoma-derived cells, computing allelic fractions from both total and polysome-associated RNA from RNA-Seq data. Allelic imbalance in polysomal RNA led us to nominate 52 coding variants associated with allele-specific mRNA translation, of which 16 are nonsynonymous. To validate instances of allele-specific translation, a proteomics workflow was developed that combines label-free shotgun analysis, high-pH reversed-phase peptide fractionation, and targeted parallel reaction monitoring using isotope-labeled peptide standards. Using this approach, we provide proof-of-concept validation of the heterozygous G>A, R183H missense single-nucleotide variant rs1554710467 in the eukaryotic initiation factor 4H (EIF4H) gene. The variant is present in two EIF4H alternatively spliced variants, which showed equivalent translation efficiency in HCT116 cells but differ in abundance. The alternative peptide containing H183 was significantly more abundant than the corresponding reference peptide containing R183, consistent with the over-representation of the alternative allele in polysomal RNA in HCT116 cells. A dual-fluorescence ribosome-stalling assay confirmed the enhanced translation potential of the variant allele. The two EIF4H allelic proteins exhibited similar stability and subpolysomal localization. This study demonstrates the feasibility of using allele-specific proteomics at the endogenous protein levels by exploiting heterozygous coding variants. Overall, our approach extends the toolbox available to investigate allele-specific differences in mRNA translation potential, a relatively underexplored layer of gene expression regulation that could reveal interindividual differences in disease-relevant phenotypes. - Source: PubMed
Publication date: 2026/02/19
Hamadou Meriem HadjerAlunno LauraPeroni DanielePancher MichaelMazza FabioVenturelli TeclaBelli RominaDassi ErikRomanel AlessandroInga Alberto - Cisplatin-based chemotherapy remains a mainstay for the treatment of bladder cancer (BLCA); however, its clinical efficacy is frequently compromised by the emergence of chemoresistance, which leads to poor patient outcomes. Although known mechanisms-such as alterations in drug efflux, DNA repair, and key signaling pathways-have been implicated, they fail to fully explain the clinical complexity of cisplatin resistance, indicating that additional molecular drivers remain undiscovered. Keratin 14 (KRT14), an intermediate filament protein associated with aggressive BLCA subtypes, is consistently upregulated in cisplatin-resistant tumors, yet its precise mechanistic role in resistance remains unclear. In this study, we elucidate the functional contribution of KRT14 to cisplatin resistance in BLCA using patient-derived tissues, established cell lines, xenograft mouse models, and a suite of molecular interaction assays. Our results demonstrate that KRT14 is significantly upregulated in BLCA tissues, correlates with poor clinical prognosis, and functionally drives cisplatin resistance both in vitro and in vivo. Mechanistically, we identify a novel and direct interaction between KRT14 and the translation initiation factor eIF4H, specifically through the N-terminal Head domain of KRT14. This interaction modulates the association of eIF4H with the core eIF4F complex, thereby selectively promoting the translation of Acyl-CoA Oxidase 2 (ACOX2) mRNA through its 5' untranslated region. We further show that ACOX2 is essential for mediating the effects of KRT14 on lipid metabolism, cell proliferation, survival, and ultimately, cisplatin resistance. Collectively, our findings reveal that KRT14 contributes to chemoresistance in BLCA not only via its structural roles but also by directly regulating translational machinery through eIF4H, leading to upregulation of the metabolic enzyme ACOX2. The newly defined KRT14-eIF4H-ACOX2 axis orchestrates lipid metabolic reprogramming and cell survival, underscoring the KRT14-eIF4H interface as a promising therapeutic target for overcoming cisplatin resistance in BLCA. - Source: PubMed
Publication date: 2025/12/24
Liu ShenghuaLiu TingtingYang ChenMou ZezhongZou LujiaJiang Haowen