Ask about this productRelated genes to: eIF4B antibody
- Gene:
- EIF4B NIH gene
- Name:
- eukaryotic translation initiation factor 4B
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 12q13.13
- Locus Type:
- gene with protein product
- Date approved:
- 1991-03-04
- Date modifiied:
- 2015-08-25
Related products to: eIF4B antibody
Related articles to: eIF4B antibody
- One of the most challenging issues in current assisted reproductive technology is how to optimally counsel and treat patients with poor ovarian response (POR). However, current research predominantly emphasized the ovarian local changes during controlled ovarian hyperstimulation, and the hypothalamic-pituitary-ovarian (HPO) axis as an integrated system in the context of clinical ovulation induction and POR remains underexplored. Investigating the inter-organ interactions and dynamic regulatory characteristics of the HPO axis in response to exogenous gonadotropin stimulation may provide molecular insights into the interaction networks of the HPO axis, and ultimately propose new potential targets for the clinical diagnosis and treatment of ovulatory disorders and POR. - Source: PubMed
Publication date: 2026/03/23
Sun JianLu MinghuiYang ChaoyanCheng YixiaoXu PeiwenZhao RusongGao Yuan - Highly metastatic cancer cells depend on polyunsaturated fatty acids (PUFAs) to enhance membrane fluidity, yet this adaptive advantage concurrently renders them more susceptible to ferroptosis. However, the adaptation and survival strategies of metastatic gastric cancer (GC) cells under severe stress conditions remain unclear. To identify driver genes underlying peritoneal metastasis (PM) in GC, we performed integrated multi-omics analyses of GC tissues, followed by validation using a large cohort of clinical samples (n = 124) and corresponding prognostic data. Both in vitro and in vivo functional studies confirmed that ChaC2 is a critical driver of PM from GC. Mechanistic investigations revealed that ChaC2 attenuates ferroptosis sensitivity caused by elevated PUFAs levels in metastatic GC cells. Under hypoxic conditions, HIF-1α transcriptionally upregulates eIF4B and promotes cytoplasmic translocation of PABP1, leading to liquid-liquid phase separation (LLPS) of the PABP1/eIF4B complex. This phase-separated structure recruits G3BP1 to nucleate stress granules (SGs), within which ChaC2 mRNA is selectively sequestered, thereby enhancing its stability and translational efficiency. Collectively, our findings demonstrate that hypoxia-induced PABP1/eIF4B LLPS specifically upregulates ChaC2 expression, enabling metastatic cancer cells to evade ferroptosis triggered by their own metastatic demands and ultimately facilitating tumor dissemination. This study uncovers a critical adaptive regulatory mechanism employed by metastatic GC cells to cope with stress challenges during PM, thereby offering novel therapeutic targets and strategic insights for intervention. - Source: PubMed
Publication date: 2026/03/02
Lin ZaihuanGao YukeZhang QiYang SaixuanChen YabangDing HanluPeng WenxuZhang XinyinNurzat YeltaiHu JulongLiao WenjingXiong BinXiao MangZhang Xiaowen - African swine fever virus (ASFV) is a highly contagious and lethal double-stranded DNA virus that relies on host cellular translation machinery for replication and immune evasion. The multigene family 110 (MGF110) contains several members with incompletely defined functions. Here, the role of MGF110-7L in host translation regulation was investigated in HEK-293T and PK15 cells. Ribopuromycylation assays demonstrated that MGF110-7L expression resulted in potent, dose- and time-dependent inhibition of nascent polypeptide synthesis. Western blotting revealed a selective reduction in eIF4G1 protein abundance, with no significant changes in eIF4G2, eIF4E, and eIF4A, while eIF4G1 mRNA levels remained unaffected, indicating post-transcriptional regulation. Overexpression of eIF4G1 partially rescued translation suppression. MGF110-7L also decreased eIF4B phosphorylation and activated the PERK/eIF2α pathway, consistent with the induction of endoplasmic reticulum (ER) stress. ER stress promoted stress granule (SG) formation and enhanced eIF4G1 association with the SG marker G3BP1. The inhibitor assays demonstrated that the suppression of eIF2α phosphorylation by ISRIB restored the abundance of eIF4G1 protein. In addition, the downregulation of eIF4G1 was reversed by the inhibition of autophagy using bafilomycin A1, indicating an SG-linked autophagy-lysosome degradation pathway. Co-immunoprecipitation assays confirmed increased eIF4G1-G3BP1 interaction, but no direct binding between MGF110-7L and eIF4G1. This work provides the first experimental evidence that an ASFV protein, MGF110-7L, suppresses cap-dependent translation through SG-mediated autophagic degradation of eIF4G1, thereby revealing a previously unrecognized mechanism of ASFV translational control. These findings not only extend current understanding of ASFV-host interactions but also suggest potential molecular targets for antiviral strategies and rational vaccine design. - Source: PubMed
Publication date: 2026/02/12
Gao XinyuJiang SuduoZhang LiyanGao ZhenqiuXiao LijieCao Hongwei - Colorectal cancer (CRC) is the third most common malignant tumor and the second leading cause of cancer-related mortality globally. Epithelial to mesenchymal transition (EMT) contributes to CRC metastasis and poor prognosis. Aberrant protein phosphorylation is implicated in CRC progression, warranting further investigation into its molecular mechanisms. Herein, we have identified significant alterations in protein phosphorylation associated with CRC through tandem mass tag (TMT) label-based phosphoproteomic analysis. The functions and enriched signaling pathways of these proteins were predominantly linked to the EMT process. Notably, the phosphorylation of eIF4B at Ser93 exhibited the most pronounced increase in CRC, a finding that was further validated in CRC tissues and cell lines by a newly generated antibody targeting eIF4B Ser93 phosphorylation. Phosphorylation of eIF4B Ser93 promoted CRC progression and metastasis both in vitro and in vivo. Mechanistically, eIF4B Ser93 phosphorylation decreased ubiquitination-mediated eIF4B degradation and enhanced its translation activity, through which it facilitated the translation of mesenchymal markers. Additionally, ERK2 directly phosphorylated eIF4B at Ser93, while inhibiting this phosphorylation is essential for the anti-cancer efficacy of the ERK2 inhibitor, Vx-11e. Together, the phosphorylation of eIF4B Ser93 driven by ERK2 promotes CRC growth and metastasis through the activation of EMT. Our findings indicate a novel therapeutic target and provide promising strategies for clinical intervention in human CRC. - Source: PubMed
Publication date: 2026/01/05
Wen SiqiLin MinZhang ManLi ZhaoChen JinchiYi BeiLiu DejunChen RuiqiChen TianyuLiang RongJiang Wei - Cytokine release syndrome (CRS) is a potentially life-threatening inflammatory condition. However, the defining features that distinguish it from self-resolving inflammation remain poorly understood. In this study, we identified monocyte/macrophage hyper-translation as a hallmark of CRS pathogenesis in patient samples. To uncover the molecular drivers of this phenomenon, a CRISPR screen followed by genetic validation pinpointed BCAP as a critical regulator of hyper-translation. Mechanistically, BCAP activated the RSK-EIF4B axis, fueling hyperactive translation in macrophages. Genetic ablation of RSK attenuated CRS-associated inflammation, and pharmacological inhibition of RSK alleviated CRS symptoms in a humanized mouse model. These findings establish hyper-translation as a key pathogenic feature of CRS and highlight protein translation as a druggable pathway, opening venues for therapeutic interventions of CRS and other inflammatory diseases. - Source: PubMed
Publication date: 2025/12/30
Liu XingxianLi JiaqiZhang YajingLiu YangWang ChunmengWang YaoLiu YunqiYang YuzhuoSu YaoLu YouxueWang WenyanFu Yang-XinLin XinPan DengHan WeidongHu Xiaoyu