EIF4B

Last update 08 May 2025

Basic Info

Synonyms

eIF-4B, EIF4B, eukaryotic translation initiation factor 4B

Introduction

Required for the binding of mRNA to ribosomes. Functions in close association with EIF4-F and EIF4-A. Binds near the 5'-terminal cap of mRNA in presence of EIF-4F and ATP. Promotes the ATPase activity and the ATP-dependent RNA unwinding activity of both EIF4-A and EIF4-F.

100 Clinical Results associated with EIF4B

100 Translational Medicine associated with EIF4B

0 Patents (Medical) associated with EIF4B

453

Literatures (Medical) associated with EIF4B

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 Apr 2025·Advanced Science

Intestinal Gastrin/CCKBR Axis Protects against Type 2 Diabetes by Reducing Intestinal Glucose Absorption through the PI3K/Akt/eIF4B Signaling Pathway

Article

Author: Liu, Yunpeng ; Liu, Xing ; Wei, Qiang ; Lu, Shuaibing ; Zhang, Haizeng ; Yang, Zhiwei ; Jose, Pedro A ; Long, Anxiong ; Liu, Wei ; Wu, Xianxian ; Sun, Shiyun ; Jiang, Xiaoliang ; Liu, Xue ; Jia, Xiaodi

AbstractThe Gastrin/CCKBR axis is essential for inhibiting intestinal sodium absorption, but its effects on intestinal glucose metabolism remain elusive. This study aims to determine the role of intestinal Gastrin/CCKBR on glucose absorption in the development of type 2 diabetes (T2D). Intestinal epithelial cell‐specific Cckbr knockout mice and control wild‐type mice are fed normal diet (ND, 10% fat) or high fat diet (HFD, 60% fat) to study the effect of intestinal Gastrin/CCKBR on blood glucose levels. Gastrin‐SiO2 microspheres (20 mg kg−1 d−1) are designed so that gastrin specifically stimulates intestinal CCKBR, without its absorption into the circulation. Mice with silenced intestinal Cckbr has pre‐diabetes mellitus (Pre‐DM) that rapidly progressed into T2D when fed HFD. Moreover, Gastrin‐SiO2 microspheres markedly reduce glucose absorption in duodenum obtained from patients with T2D. In mice with HFD‐induced T2D, Gastrin‐SiO2 microspheres reduce intestinal glucose absorption by down‐regulating intestinal SGLT1 and GLUT2 expressions and stimulating incretin secretion. This study shows the important role of intestinal Gastrin/CCKBR in intestinal glucose absorption. Gastrin‐SiO2 microspheres may be a promising strategy for the treatment of patients with T2D.

01 Apr 2025·Cancer Letters

YTHDF3 drives tumor growth and metastasis by recruiting eIF4B to promote Notch2 translation in breast cancer

Article

Author: Lou, Kangliang ; Qiao, Zishan ; Chen, Hongyu ; Pei, Yifei ; Zhang, Guojun ; Bai, Jingwen ; Lin, Linling ; He, Yueyang ; Li, Chengxi ; Gao, Yiyang ; Yang, Lulin

YTH domain family protein 3 (YTHDF3), an m⁶A RNA reader, is implicated in various cancers, but its role in breast cancer progression and metastasis remains unclear. In this study, we explore the oncogenic potential of YTHDF3 in breast cancer, focusing on its impact on epithelial-mesenchymal transition (EMT) and metastasis. We found that YTHDF3 is significantly upregulated in breast cancer tissues and associated with poor relapse-free survival (RFS). Functional studies demonstrated that YTHDF3 promotes EMT in breast cancer cell lines by enhancing cell migration, invasion, and metastasis in vivo. Mechanistically, we show that YTHDF3 regulates Notch2, a key driver of EMT, through an m⁶A-dependent mechanism. YTHDF3 binds to m⁶A-modified Notch2 mRNA and recruits eIF4B to facilitate its translation, leading to increased Notch2 translation and subsequent inducing EMT. Our findings highlight the importance of the YTHDF3-Notch2 axis in driving EMT and metastasis in breast cancer. Furthermore, targeting YTHDF3 with lipid nanoparticles (LNPs) encapsulating siRNA and indocyanine green (ICG) significantly suppressed tumor growth and lung metastasis while enabling real-time therapeutic monitoring via ICG fluorescence imaging. These findings establish YTHDF3 as a critical driver of EMT and metastasis through m⁶A-dependent Notch2 translation, highlighting its potential as a therapeutic target in breast cancer.

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EIF4B

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