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EIF4G2-mediated Translation Initiation of Histone Modifiers is Essential for Intestinal Stem Cell Maintenance and Differentiation [RNA-seq]

ABSTRACT: 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.

ORGANISM(S): Mus musculus

PROVIDER: GSE294512 | GEO | 2026/04/30

REPOSITORIES: GEO

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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

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

2026-04-30 | GSE318066 | GEO

eIF4G2-Mediated Translation Initiation of Histone Modifiers is Essential for Intestinal Stem Cell Maintenance and Differentiation

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

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.

2020-10-19 | GSE158136 | GEO

Nat1 promotes translation of specific proteins that induce differentiation of mouse embryonic stem cells [ribosome profiling]

Project description:Nat1 (also known as p97/Dap5/Eif4g2) is a ubiquitously expressed cytoplasmic protein that is homologous to the C-terminal two thirds of eukaryotic translation initiation factor 4G (also known as Eif4g1). We previously showed that Nat1-null mouse embryonic stem cells (mESCs) were resistant to differentiation. In the current study, we found that Nat1 and Eif4g1 share many binding proteins, such as Eif3s, Eif4s and ribosomal proteins. However, Nat1 did not bind to Eif4e or poly A binding proteins, which are critical for cap-dependent translation initiation. In contrast, Nat1 binds to Eif2s, Fmr and related proteins, and Prrc2 proteins more preferentially than does Eif4g1. We also found that Nat1-null mESCs possess a status partially similar to ground state, which is established in wild-type mES cells when treated with inhibitors of the ERK and GSK3 signaling pathways. In Nat1-null mESCs, the ERK pathway is suppressed even without inhibitors. Ribosomal profiling revealed that translation of Map3k3 and Sos1 is suppressed in the absence of Nat1. Forced expression of Map3k3 induced differentiation of Nat1-null mESCs. These data collectively showed that Nat1 is involved in translation of proteins that are required for cell differentiation.

2017-01-06 | GSE89011 | GEO

Nat1 promotes translation of specific proteins that induce differentiation of mouse embryonic stem cells [expression]

2017-01-06 | GSE89007 | GEO

Nat1 promotes translation of specific proteins that induce differentiation of mouse embryonic stem cells [expression 2]

Project description:Nat1 (also known as p97/Dap5/Eif4g2) is a ubiquitously expressed cytoplasmic protein that is homologous to the c-terminal two thirds of eukaryotic translation initiation factor 4G (also known as Eif4g1). We previously showed that Nat1-null mouse embryonic stem cells (mESCs) were resistant to differentiation. In the current study, we found that NAT1 and eIF4G1 share many binding proteins, such as eIF3, eIF4A and ribosomal proteins. However, NAT1did not bind to eIF4E or poly A binding proteins, which are critical for cap-dependent translation initiation. In contrast, compared to eIF4G1, NAT1 preferentially interacts with eIF2, FMR and related proteins, and especially PRRC2 family members. We also found that Nat1-null mESCs possess a transcriptional profile similar, though not identical, to ground state, which is established in wild-type mES cells when treated with inhibitors of the ERK and GSK3 signaling pathways. In Nat1-null mESCs, the ERK pathway is suppressed even without inhibitors. Ribosome profiling revealed that translation of Map3k3 and Sos1 is suppressed in the absence of Nat1. Forced expression of Map3k3 induced differentiation of Nat1-null mESCs. These data collectively showed that Nat1 is involved in translation of proteins that are required for cell differentiation.

2017-01-06 | GSE89600 | GEO

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

Proteomic profiling of in vitro differentiated WT and eIF4G2 knockout B cells

Project description:eIF4G2 (also known as DAP5 or NAT1) is a translation initiation factor. By generating Eif4g2fl/fl;Cγ1-Cre mice, in which the expression of Cre recombinase is induced by transcription of the Ig gamma1 constant region gene segment and deletes Eif4g2 in activated B cells, we found eIF4G2 is essential for plasma cell differentiation. The experiment aimed to identify changes in the global proteome resulting from the deletion of eIF4G2.

2025-11-26 | PXD071241 |

eIF4G2 cross-linking immunoprecipitation (CLIP) in primary cortical neurons

Project description:Learning and memory require activity-induced changes in mRNA translation within dendrites, but which mRNAs are involved and how they are regulated remain unclear. We combined proximity labeling with ribosome profiling and CLIP to monitor how depolarization impacts dendritic translation. For a functionally coherent set of transcripts highly enriched in mitochondrial genes, depolarization leads to enhanced uORF translation, eIF4G2 binding, and increased translation. Engineered reporters demonstrate that activity-dependent translational control is conferred by the 5’UTRs and that dendritic localization, eIF4G2 binding, and uORF translation are necessary and sufficient to mediate this regulation. Downstream, this drives activity-dependent changes in dendritic mitochondrial function. Our studies uncover an unanticipated mechanism by which activity-dependent uORF translational control by eIF4G2 enables the coupling of synaptic activity to local remodeling of dendrites.

2024-03-14 | GSE213082 | GEO

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