Ask about this productRelated genes to: EIF3H Blocking Peptide
- Gene:
- EIF3H NIH gene
- Name:
- eukaryotic translation initiation factor 3 subunit H
- Previous symbol:
- EIF3S3
- Synonyms:
- eIF3-gamma, eIF3-p40, eIF3h
- Chromosome:
- 8q23.3-q24.11
- Locus Type:
- gene with protein product
- Date approved:
- 1998-11-26
- Date modifiied:
- 2018-02-13
Related products to: EIF3H Blocking Peptide
Related articles to: EIF3H Blocking Peptide
- Reliable normalization is essential for accurate quantitative real-time PCR (qRT-PCR) analysis, yet suitable reference genes have not been systematically evaluated in , an emerging marine experimental fish used in physiological and environmental research. In this study, 17 candidate reference genes were evaluated in five tissues (brain, gill, gonad, intestine, and liver) of sexually mature male and female under solvent control (DMSO), bisphenol A (BPA), cadmium (Cd), and sulfamethazine (SMX) treatment conditions. Gene-expression stability was assessed using the comparative ΔCt method, NormFinder, geNorm, BestKeeper, and the integrated RefFinder ranking. The results showed that reference-gene stability was strongly tissue-specific and analysis-dependent. The integrated RefFinder analysis identified , , , , and as the most stable genes in the pooled dataset, whereas , , and were the least stable. geNorm analysis indicated that two reference genes were sufficient for brain, gill, intestine, and liver, whereas four were required for the gonad and six for cross-tissue comparisons. These findings provide the first systematic basis for reference-gene selection in and establish an important methodological foundation for future qRT-PCR studies in this species, particularly in research on endocrine disruption, reproductive physiology, and marine ecotoxicology. - Source: PubMed
Publication date: 2026/05/05
Dong ZhongdianGao JiahaoLi XiaobinChen ZhishanLi JianjunLiao JianZhang YanpingWang ZhongduoGuo YusongZhang Ning - Pancreatic adenocarcinoma (PAAD) ranks among the most lethal human solid tumors, distinguished by its swift progression and limited effective treatment options. The eukaryotic translation initiation factor 3 subunit H (EIF3H) is postulated to be a critical factor in translational initiation, with emerging research indicating its potential involvement in promoting tumor invasion and metastasis. Nevertheless, the precise role of EIF3H within tumors remains insufficiently understood. - Source: PubMed
Publication date: 2026/02/25
Sun KaiSong Zhi-XinZhang Xiao-YunWang Xue-XingWen SongWang Ke-RunQiu Yi-Lian - The Src oncogene controls cancer cell invasiveness by promoting invadosome formation and extracellular matrix (ECM) degradation. Invadosomes are translational hotspots enriched in the eukaryotic translation initiation factor 3 (eIF3) complex that is mandatory for their maintenance. Here, we determined that Src regulates mRNA translation and controls the expression of eIF3 subunits, including eIF3h, eIF3e, and eIF3d. These subunits are crucial for invadosome formation and ECM degradation. Src also modulates both canonical eIF4E-dependent translation via the activation of the phosphoinositide-3-kinase (PI3K)/AKT/mammalian target of rapamycin (mTOR) pathway and the non-canonical translation mechanism through eIF3d overexpression, both of which are necessary for invadosome function. Moreover, overexpression of Src and eIF3h/e/d correlates with poor prognosis in patients with hepatocellular carcinoma (HCC), promoting ECM degradation and tumor invasiveness of HCC cells. This study identifies Src as a major regulator of translation initiation, modulating invadosome formation, ECM degradation, and tumor cell invasion. - Source: PubMed
Publication date: 2026/02/23
Bonnard BenjaminChatefau AnoukDourthe CyrilDi Tommaso SylvaineDupuy Jean-WilliamMahouche IsabelleSolorzano JacoboLe Bras MorganeRaymond Anne-AurélieMoreau ViolaineJabouille ArnaudBlangy AnneMartineau YvanSaltel Frédéric - Cells adapt to proteostatic and metabolic stresses, in part, through stress activated eIF2α kinases that stimulate the translation of ATF4. Stress-induced ATF4 translation is regulated through elements at ATF4 mRNA's 5' leader. In addition to eIF2α kinases, ATF4 induction requires other regulators that remain poorly understood. Here, we report an ATF4 regulatory network consisting of eIF4E-Homologous Protein (4EHP), NELF-E, the 40S ribosome, and eIF3 subunits. Specifically, we found that the mRNA cap-binding protein, 4EHP, was required for ATF4 signaling in the Drosophila larval fat body and in disease models associated with abnormal ATF4 signaling. NELF-E mRNA, encoding a regulator of pol II-mediated transcription, was identified as a top interactor of 4EHP in a TRIBE (Targets of RNA Binding through Editing) screen. Quantitative proteomics analysis revealed that the knockdown of NELF-E or 4EHP commonly reduced several subunits of the 40S ribosome (RpS) and the eIF3 translation initiation factor. Moreover, reduction of NELF-E, 4EHP, RpS12, eIF3l, or eIF3h suppressed the expression of ATF4 and its target genes. These results uncover a previously unrecognized ATF4 regulatory network consisting of 4EHP and NELF-E that impacts proteostasis during normal development and in disease models. - Source: PubMed
Publication date: 2025/12/23
Walsh KristofferKatow HidetakaJunn HannahVasudevan DeepikaDieterich ChristophRyoo Hyung Don - The resistance to oxaliplatin (OXA)-based chemotherapies may lead to poor prognosis in patients with gastric cancer (GC). Emerging evidence suggests that resistance is closely associated with phosphorylation modifications. In GC cell line AGS, high-throughput base editor screen identified key phosphorylation sites associated with OXA response. Methyltransferase-like 3 (METTL3) S2 emerged as a notable negative hit. Further investigation revealed that dephosphorylation of METTL3 S2 disrupted the METTL3-eukaryotic translation initiation factor 3 subunit H (eIF3H) interaction, thereby suppressing the translation of oncogenes involved in replication stress responses, including bromine domain protein 4 () and serpin family E member 2 (), ultimately enhancing sensitivity to OXA. In addition, clinical investigation showed that METTL3 S2 phosphorylation was highly correlated with the response to GC OXA chemotherapy. In summary, base editor screen provides a versatile approach for exploring the role of phosphorylation sites in cancer chemotherapy. The METTL3-eIF3H interaction may serve as a potential therapeutic target. - Source: PubMed
Publication date: 2025/12/12
Xu XiaoranTao WanyuLiu YixinGuo TangxiZhang YuWei DongyiYan PichengHuang XingxuWei Yongchang