Request Demo

Last update 08 May 2025

EIF4G2

Last update 08 May 2025

Basic Info

Synonyms

DAP-5, DAP5, Death-associated protein 5

+ [7]

Introduction

Appears to play a role in the switch from cap-dependent to IRES-mediated translation during mitosis, apoptosis and viral infection. Cleaved by some caspases and viral proteases.

Drugs associated with EIF4G2

HG-1026

Target

DAP x EIF4G2 x HPRT1

Mechanism

DAP gene modulators [+2]

Active Org.-

Originator Org.

Human Genome Sciences, Inc.

Active Indication-

Inactive Indication-

Drug Highest PhasePending

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with EIF4G2

100 Translational Medicine associated with EIF4G2

0 Patents (Medical) associated with EIF4G2

207

Literatures (Medical) associated with EIF4G2

31 Dec 2025·RNA Biology

Sorafenib-associated translation reprogramming in hepatocellular carcinoma cells

Article

Author: de la Cruz, Jesús ; Rodríguez-Gil, Alfonso ; Contreras, Laura ; Muntané, Jordi

Sorafenib (Sfb) is a multikinase inhibitor regularly used for the management of patients with advanced hepatocellular carcinoma (HCC) that has been shown to increase very modestly life expectancy. We have shown that Sfb inhibits protein synthesis at the level of initiation in cancer cells. However, the global snapshot of mRNA translation following Sorafenib-treatment has not been explored so far. In this study, we performed a genome-wide polysome profiling analysis in Sfb-treated HCC cells and demonstrated that, despite global translation repression, a set of different genes remain efficiently translated or are even translationally induced. We reveal that, in response to Sfb inhibition, translation is tuned, which strongly correlates with the presence of established mRNA cis-acting elements and the corresponding protein factors that recognize them, including DAP5 and ARE-binding proteins. At the level of biological processes, Sfb leads to the translational down-regulation of key cellular activities, such as those related to the mitochondrial metabolism and the collagen synthesis, and the translational up-regulation of pathways associated with the adaptation and survival of cells in response to the Sfb-induced stress. Our findings indicate that Sfb induces an adaptive reprogramming of translation and provides valuable information that can facilitate the analysis of other drugs for the development of novel combined treatment strategies based on Sfb therapy.

01 Jul 2025·Gene

The proximity proteome of pre-40S pre-ribosomal particle components PNO1 and NOB1 using turboID proximity labeling technology

Article

Author: Zheng, Jiefu ; Xu, Xingyuan ; Zhu, Shuang ; Yan, Haiyan ; Liao, Jian-You ; Chen, Wenli

BACKGROUNDThe ribosome assembly factors PNO1 and NOB1 play crucial roles in the maturation of the 40S ribosomal small subunit. TurboID is an efficient biotin ligase that can biotinylate proteins in proximity to the target protein and is widely used to study complex biological processes within cells. In this study, we employed this technology to investigate the complex proximity network of PNO1 and NOB1 within the cell, further revealing their key roles in ribosome biogenesis.RESULTSFirstly, through immunofluorescence experiments, we observed that PNO1 and NOB1 have different localizations within the cell. Subsequently, by analyzing the proximal proteins labeled by PNO1-TurboID and NOB1-TurboID, we identified 871 proximal proteins for PNO1 and 1044 for NOB1, with 663 overlapping proteins. Functional analysis revealed that these proximal proteins are predominantly enriched in biological processes related to ribosome assembly, rRNA processing, and translation, all of which are closely linked to ribosome biogenesis. Notably, we validated the mass spectrometry-identified proteins through co-IP experiments and found that PNO1 and NOB1 interact with the translation-related proteins EIF4B and EIF4G2.CONCLUSIONOur study constructed the protein network environment of ribosome assembly factors PNO1 and NOB1 within the cell and found that their neighboring proteins are primarily involved in key biological processes such as ribosome processing, mRNA translation, and the cell cycle, all of which are critical for ribosome biogenesis. These findings provide a valuable foundation for further understanding the roles of PNO1 and NOB1 in ribosome biogenesis and how they regulate this process.

01 May 2025·Developmental Biology

A critical genetic interaction between Gemin3/Ddx20 and translation initiation factor NAT1/eIF4G2 drives development

Article

Author: Cacciottolo, Rebecca ; Cauchi, Ruben J

Gemin3 (Gem3) or DEAD-box RNA helicase 20 (Ddx20) has been mostly implicated in the assembly of spliceosomal small nuclear ribonucleoproteins (snRNPs) as part of the SMN-Gemins complex. Nonetheless, several studies have hinted at its participation in diverse snRNP-independent activities. Here, we utilised a narrow unbiased genetic screen to discover novel Gem3 interactors in Drosophila with the aim of gaining better insights on its function in vivo. Through this approach, we identified a novel genetic interaction between Gem3 and NAT1, which encodes the Drosophila orthologue of translational regulator eIF4G2. Despite lack of a physical association, loss of NAT1 function was found to downregulate Gem3 mRNA levels. Extensive convergence in transcriptome alterations downstream of Gem3 and NAT1 silencing further supports a functional relationship between these factors in addition to showing a requirement for both in actin cytoskeleton organisation and organism development, particularly neurodevelopment. In confirmation, flies with either Gem3 or NAT1 depletion exhibited brain growth defects and reduced muscle contraction. Severe delays in developmental progression were also observed in a newly generated Gem3 hypomorphic mutant. Our data linking Gemin3 to a key component of the translational machinery support an emerging role for Gemin3 in translation that is also critical during organism development.

Analysis

Perform a panoramic analysis of this field.

view full example data

Hiro LS Researcher

The AI Search Engine Built to Accelerate Biopharma Decisions

Search across billion-scale life sciences data to uncover signals, validate evidence, and act with confidence.

Ask any biopharma research question→

Get started for free today!

Accelerate Strategic R&D decision making with Synapse, Patsnap’s AI-powered Connected Innovation Intelligence Platform Built for Life Sciences Professionals.

Discover Synapse Data Servers

Synapse data is now integrated into the PatSnap LS Model Context Protocol (MCP) service. Customize your LLM agent now using our MCP server!

Bio

Bio Sequences Search & Analysis

Chemical

Chemical Structures Search & Analysis

EIF4G2

Basic Info

Related

Analysis