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Loss of EIF4G2 Mediates Aggressiveness in Distinct Endometrial Cancer Subpopulations with Adverse Outcomes in Patients

ABSTRACT: Low EIF4G2 protein expression was shown to have a poor OS of endometrial patients. Control and EIF4G2KD HEC-1A cells were sorted using CD133 merker to CD133+ and CD133- populations. These populations were taken to RNAseq and MS analysis to explore the mechanism.

ORGANISM(S): Homo sapiens

PROVIDER: GSE242717 | GEO | 2024/02/18

REPOSITORIES: GEO

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Loss of EIF4G2 Mediates Aggressiveness in Distinct Endometrial Cancer Subpopulations with Adverse Outcomes in Patients

Project description:Loss of EIF4G2 Mediates Aggressiveness in Distinct Endometrial Cancer Subpopulations with Adverse Outcomes in Patients

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EIF4G2 Promotes HCC Progression

Project description:Aberrant translation from mRNAs to proteins plays a crucial role in the pathogenesis of various cancers. Here, we revealed that the key proteins involved in translation were up-regulated in two hepatocellular carcinoma (HCC) cohorts. Specifically, we identified the translation initiation factor EIF4G2 as a marker of poor prognosis, linked to unfavorable overall survival (OS) outcomes. Our in vitro and in vivo studies confirmed that EIF4G2 promotes the development and metastasis of HCC. As an essential translation initiation factor, EIF4G2 knockdown disrupts polyribosome stability and inhibits nascent protein synthesis in the Huh-7 and MHCC97H cell lines. By com-paring the proteome and transcriptome of Huh-7 cells, we further identified PLEKHA1 as an essential target of EIF4G2 with IRES-dependent translation. PLEKHA1 was able to rescue the inhibitory effects of EIF4G2 knockdown on cell migration and invasion in both Huh-7 and MHCC97H cells. This research provides novel insights into the critical role of EIF4G2-dependent translation in cancer, where PLEKHA1 promotes HCC progression.

2024-05-30 | PXD052695 |

eIF4G2-dependent translation restrains pancreatic cancer progression

Project description:Pancreatic ductal adenocarcinoma (PDA) is among the most lethal cancers, driven by cellular plasticity that fuels therapeutic resistance and early dissemination. The contribution of translational control to this plasticity remains poorly understood. Through an in vivo CRISPR/Cas9 screen, we identify the non-canonical initiation factor eIF4G2 (DAP5/NAT1) as a translational checkpoint restraining PDA progression. Loss of eIF4G2 accelerated tumor growth, induced poorly differentiated, basal-like histology, and triggered widespread metastatic spread. Ribosome profiling revealed that eIF4G2 loss did not increase bulk protein synthesis but instead suppressed translation of a selective regulon, including tumor suppressors such as PTEN and CREBBP. Functional studies confirmed that PTEN loss was sufficient to drive dedifferentiation but insufficient to promote metastasis, implicating the broader eIF4G2-dependent program—including translational control of transcriptional regulators like CREBBP—in limiting dissemination. Consistently, eIF4G2-deficient tumors showed transcriptomic enrichment of migratory and stemness programs. Computational inference from human PDA datasets demonstrated reduced eIF4G2 activity in metastases, aligning with basal-like features and predicting poorer survival. These results define eIF4G2 as a translational regulator that maintains epithelial identity and restrains metastatic potential, highlighting selective translation as a determinant of PDA subtype and clinical outcome.

2026-04-13 | GSE308769 | GEO

Loss of EIF4G2 mediates aggressiveness in distinct human endometrial cancer subpopulations with poor survival outcome in patients.

Project description: Not available

| S-EPMC10997518 | biostudies-literature

Transcriptomes Sequencing of si-EIF4G2 and si-NC groups in Hep3B cells

Project description:We transfected siRNA-EIF4G2 and si-NC into Hep3B cells to explore the differentially expressed genes in cells and the affected intracellular signaling pathways after EIF4G2 knockdown

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Ribo-seq data from NIH 3T3 cells lacking eIF4G2

Project description:Eukaryotic translation initiation factor (eIF) 4G2 is a long-known homologue of the canonical eIF4G1. However, unlike the latter, it does not bind eIF4E or PABP, thus it remains unclear what and when brings eIF4G2 onto a ribosome. Here we report results of ribosome profiling performed in NIH 3T3 eIF4G2 (DAP5) -/- cells.

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eIF4G2-dependent translation of pro-fibrotic mRNAs is essential for cardiac fibroblast activation (RIP-Seq)

Project description:RNA-binding proteins control gene expression in cardiac fibroblasts during TGFb-driven fibrotic responses, including the eukaryotic translation initiation factor 4G2 (eIF4G2), which was known to facilitate alternative mRNA translation during cellular stresses. However, the precise role of eIF4G2 in cardiac fibroblast activation in response to fibrotic stress remains unclear. In this study, we found increased eIF4G2 protein levels in the hearts of heart failure patients and myocardial infarcted mice, as well as in TGFb-treated immortalized human and primary mouse cardiac fibroblasts. Depletion of eIF4G2 led to predominant translational downregulation of genes that are enriched in focal adhesion and extracellular matrix pathways. eIF4G2 knockdown reduced the proliferation, migration, and collagen secretion of TGFb-treated cardiac fibroblasts. Mechanistically, we found that the translation of IGFBP7 mRNA relies on eIF4G2, which is crucial for ECM production in response to pro-fibrotic stimuli. The interaction between eIF4G2 and a DEAD box RNA helicase DDX24 can regulate IGFBP7 protein expression in cardiac fibroblasts. Together, these findings suggest that the TGFb-eIF4G2-IGFBP7 axis establishes a novel translational regulatory circuit that governs cardiac fibroblast activation. Furthermore, conditional knockout of Eif4g2 in POSTN-positive myofibroblasts reduced cardiac fibrosis in the myocardial infarction mouse model, thus improving cardiac function. Our study provides insights into the molecular mechanism of eIF4G2-mediated translational regulation of crucial physiological mRNAs during cardiac fibroblast activation.

2024-07-31 | GSE239824 | GEO

eIF4G2-dependent translation of pro-fibrotic mRNAs is essential for cardiac fibroblast activation (Polysome-Seq)

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Project description:eIF4G2 (also known as NAT1, p97, or DAP5) is an evolutionally conserved protein homologous to the C-terminal two-thirds portion of eukaryotic translation initiation factor (eIF) 4G. Despite its abundant and ubiquitous expression, the physiological and pathological functions of eIF4G2 are poorly understood. Here, we show that acute inactivation of eIF4G2 in adult mice results in rapid weight loss with abnormalities in multiple organs. Genome-wide ribosome profiling revealed that eIF4G2 is critical for the translation of key histone modification proteins involved in the maintenance and differentiation of intestinal stem cells. Our study underscores the importance of eIF4G2-mediated translation in multicellular organisms.

2026-04-24 | GSE294619 | GEO

eIF4G2-mediated Translation Initiation of Histone Modifiers is Essential for Intestinal Stem Cell Maintenance and Differentiation [Multiome]

Project description:eIF4G2 (also known as NAT1, p97, and DAP5) is an evolutionally conserved protein homologous to the c-terminal two thirds portion of eukaryotic translation initiation factor (eIF) 4G. Despite its abundant and ubiquitous expression, physiological and pathological functions of eIF4G2 are poorly understood. Here we show that acute inactivation of eIF4G2 in adult mice results in rapid weight loss with abnormalities in multiple organs. In this study, we show that eIF4G2 is critical for translation of key histone modification proteins involved in maintenance and differentiation of intestinal stem cells. Our study underscores the importance of eIF4G2-mediated translation in multicellular organisms.

2026-04-30 | GSE318068 | GEO

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