Ask about this productRelated genes to: eIF4G antibody
- Gene:
- EIF4G3 NIH gene
- Name:
- eukaryotic translation initiation factor 4 gamma 3
- Previous symbol:
- -
- Synonyms:
- eIF4GII
- Chromosome:
- 1p36.12
- Locus Type:
- gene with protein product
- Date approved:
- 1998-11-30
- Date modifiied:
- 2016-02-03
Related products to: eIF4G antibody
Related articles to: eIF4G antibody
- Long non-coding RNAs (lncRNA) play important regulatory roles during embryonic genome activation (EGA) in porcine early embryonic development. However, whether promoter-associated lncRNAs exert key functions in EGA and their underlying regulatory mechanisms remain largely unclear in pigs. In this study, we identified a highly expressed promoter-associated long non-coding RNA during the 4-cell stage of porcine embryos and named it pancEIF4G3. pancEIF4G3 is a nuclear-localized lncRNA that lacks protein-coding capacity and exhibits an expression pattern similar to its neighboring gene EIF4G3. The study found that interference with either pancEIF4G3 or EIF4G3 led to developmental arrest of porcine embryos at the 4-cell stage, indicating their crucial role in early embryogenesis. Further investigation revealed that pancEIF4G3, which is located upstream of EIF4G3, regulates both its RNA and protein expression levels through binding to OGG1. Downregulation of pancEIF4G3 and EIF4G3 resulted in reduced chromatin accessibility, decreased nascent RNA synthesis, and significant downregulation of multiple EGA marker genes and core transcription factors. In summary, this study is the first to reveal a novel mechanism in porcine early embryos whereby the promoter-associated lncRNA pancEIF4G3 regulates the expression of the translation initiation factor EIF4G3, thereby influencing the process of embryonic genome activation. This finding enriches the regulatory network of early embryonic development in pigs and also provides a potential molecular target for optimizing in vitro embryo culture and reproductive techniques. - Source: PubMed
Publication date: 2026/04/29
He TianyaoLu HuiqinZhang ChenyuanZhang ShanlongLi HanZhang ShichaoLiu DongsongZhu YanlongSun Jing-TaoWang JiaqiangLiu ZhonghuaJin Jun-Xue - Formation of a "closed-loop" mRNP, in which the 5' cap and 3' poly(A) tail are bridged by eIF4E-eIF4G-PABP interactions, has long been proposed to drive efficient translation initiation. Direct tests of this model in mammalian cells have remained elusive. Using auxin-inducible degron (AID) technology to acutely deplete eIF4G1, we find that global translation is only partially reduced and recovers without restoration of eIF4G1 levels. We identify eIF4G3 as an underappreciated contributor to basal translation that buffers translational output upon eIF4G1 loss without increased protein expression, explaining the modest defects observed in prior RNAi-based studies. Systematic replacement of eIF4G1 with defined cleavage products and interaction mutants reveals that PABP binding by eIF4G1 is dispensable for bulk translation initiation: the central caspase-3 cleavage fragment of eIF4G1 (casp3-cp), which lacks the PABP-interaction domain, fully rescues global protein synthesis, and acute depletion of both major cytoplasmic PABP paralogs primarily destabilizes mRNAs rather than impairing initiation. In contrast, the N-terminal enteroviral 2A cleavage product (2A-cp) is a potent, dominant translational repressor that requires simultaneous eIF4E and PABP engagement to form a dead-end closed-loop mRNP that sequesters initiation factors without enabling 43S recruitment. These findings reveal that the eIF4G-PABP closed-loop architecture is not required for productive initiation but can be actively co-opted for translational silencing. This explains why viral eIF4G cleavage, but not factor depletion, produces near-complete translational shutoff. The modular architecture of eIF4G enables diametrically opposing translational outcomes through selective proteolytic processing. - Source: PubMed
Publication date: 2026/04/07
Johnston RyanBrekker Mollie AKhalil NoelleGoldstein Monty EAldrich AnneGrimins Autumn OGritli SamiMarintchev AssenBlower Michael DSaeed MohsanLyons Shawn M - The start of eukaryotic translation requires recruitment of messenger RNA (mRNA) through the action of the eukaryotic initiation factor 4F (eIF4F) complex. eIF4F is formed by joining of the eIF4G and eIF4E subunits and generally also requires the eIF4A helicase. In Leishmania infantum, five eIF4Gs form multiple eIF4F-like complexes, with those based on the related EIF4G3 and EIF4G4 being active during translation, but with likely nonredundant roles that need to be better defined. - Source: PubMed
Publication date: 2026/03/04
Oliveira Stéphanny Sallomé SousaMelo do Nascimento LarissaMoura Danielle Maria Nascimentode Souza Reis Christian Robsonde Melo Neto Osvaldo Pompílio - Sepsis, a life-threatening condition driven by a dysregulated host response, poses significant challenges for early diagnosis and early intervention. This study aimed to identify robust biomarkers capable of distinguishing sepsis from non-infectious systemic inflammation (SIRS). - Source: PubMed
Publication date: 2026/02/21
E BingChen LiaoyueLuo ShaotingXie LiangfuWang XinfengWang WeiXia YongjieYang XueFu GuibingWang Jiansheng - RNA-binding proteins (RBPs) govern mRNA fate and critically regulate spermatogenesis. The poly(rC)-binding protein 2 (PCBP2), a testis-enriched RBP, remains uncharacterized in spermatogenesis. In this study, we identified and validated PCBP2 downregulation in testicular tissues from patients with non-obstructive azoospermia (NOA) by integrating bulk and single-cell RNA sequencing (scRNA-seq) datasets. To investigate its function, we generated mice with a germline-specific ablation of Pcbp2. These mice exhibited delayed meiotic prophase and impaired spermiogenesis. Specifically, we observed a reduction in mid-pachytene spermatocytes and a distinct developmental arrest at step 9 of spermiogenesis. Mechanistically, integrated IP-MS, RNA-Seq, and RIP-Seq analyses revealed that PCBP2 recruits hnRNPU and DDX5 to key transcripts related to meiosis (Spo11, Tdrd5 and Brme1) and spermiogenesis (Eif4g3, Piwil1 and Dlec1), thereby orchestrating mRNA stability and alternative splicing of target genes. This study establishes PCBP2 as an indispensable multifunctional RBP required for meiotic progression and spermiogenesis. Our findings identify a novel mechanism of RBP-driven male infertility and indicate PCBP2 as a potential diagnostic marker and therapeutic target for NOA. - Source: PubMed
Publication date: 2026/02/06
Xiong QiaohuaQin ZihanLi YatingYim Wai YenWang ZihanTan ZhaopingTian JiarongZhang YingCao YumingZhang Yuanzhen