Ask about this productRelated genes to: eIF4B antibody
- Gene:
- EIF4B NIH gene
- Name:
- eukaryotic translation initiation factor 4B
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 12q13.13
- Locus Type:
- gene with protein product
- Date approved:
- 1991-03-04
- Date modifiied:
- 2015-08-25
Related products to: eIF4B antibody
Related articles to: eIF4B antibody
- Poly(A)-binding proteins (PABPs) are scaffold proteins that bind to the poly(A) tail of mRNAs and ensure translation fidelity by forming a closed-loop circular mRNA via association with the cap-binding complex. They can be either cytoplasmic or nuclear and play important roles in regulating polyadenylation, deadenylation, translation initiation and termination, mRNA stability, synthesis of the poly(A) tail, regulation of poly(A) length and stimulation of mRNA maturation as well as nuclear export of certain mRNAs. In higher eukaryotes, PABPs are well characterized. However, in pathogenic parasites such as trypanosomatids, belonging to the genera Leishmania and Trypanosoma, as well as Plasmodium, they are not well characterized. Using bioinformatics and computational tools, we have previously studied parasite translation initiation factors such as eIF4E, eIF4G, eIF4A, eIF4B, and Mnk1 kinase and have shown that they vary considerably and differ significantly from human translation initiation factors. In this report, the orthologues of the translation factor PABP in trypanosomatids and Plasmodium are studied. Both conservation and significant differences were observed in PABPs from these pathogenic parasites compared to human PABPs, which should prompt further structure-function studies of these proteins. - Source: PubMed
Das Supratik - Colorectal cancer (CRC) remains a major cause of cancer mortality, necessitating the identification of novel oncogenic drivers. We report the discovery of MP104, a 104-amino acid microprotein encoded by the long non-coding RNA ZEB1-AS1, which is endogenously expressed and upregulated in CRC with strong association to poor prognosis. Functional assays revealed that MP104 promotes CRC cell proliferation, migration, invasion, and metastasis. Mechanistically, MP104 interacts with UBE2O to facilitate AMPKα2 ubiquitination and degradation, thereby activating mTOR signaling. This activation enhances EIF4B phosphorylation and stability, while MP104 further inhibits RNF40-mediated EIF4B ubiquitination, collectively sustaining translational upregulation. Thus, MP104 drives CRC progression primarily through reprogramming protein translation via the UBE2O-AMPKα2-mTOR-EIF4B axis, establishing it as a key regulator of oncogenic translational control and a promising biomarker and therapeutic target in CRC. - Source: PubMed
Publication date: 2026/07/23
Chen FangWang MiaoYong HongmeiDing JinXu ShipingGe QiruiWang YanZhang LeiXiao QianqianLi BenliLin LiChu SufangWang QianqingBai JinHou Pingfu - Translation initiation requires messenger RNAs (mRNAs) to be recognized and loaded into ribosomes through a process catalyzed by the heterotrimeric eukaryotic initiation factor eIF4F. During this process, eIF4F engages the 7-methylguanosine cap at the 5' end of the mRNA and promotes productive engagement with the ribosomal pre-initiation complex (PIC) to facilitate PIC loading onto the mRNA. Although eIF4F is central to translation initiation and its regulation, the molecular mechanism by which eIF4F stimulates PIC loading, and the mechanistic role of the essential ATP hydrolysis step catalyzed by eIF4F, have remained unresolved. Here, we use single-molecule fluorescence microscopy to directly visualize the dynamics of eIF4F during cap recognition and PIC engagement. We show that ATP binding, but not ATP hydrolysis, promotes productive assembly of eIF4F on mRNA and enables dynamic redistribution of eIF4F along the transcript. In contrast, ATP hydrolysis is specifically required for recycling of cap-stalled eIF4F during productive PIC engagement. Furthermore, we identify eIF3 and eIF4B as the minimal PIC-associated factors required to stimulate ATP-hydrolysis-dependent recycling of eIF4F during PIC loading. Together, our results support a model in which productive PIC engagement stimulates ATP-hydrolysis-dependent recycling of eIF4F, thereby coupling eIF4F recycling to PIC loading during translation initiation. This mechanism provides a framework for understanding how mRNA topology, RNA-binding proteins, and the availability of initiation factors can control translational efficiency. - Source: PubMed
Publication date: 2026/06/23
Gentry Riley CIde Nicholas AComunale Victoria MAitken Colin EcheverríaKinz-Thompson Colin DGonzalez Ruben L - Chikungunya virus (CHIKV), a mosquito-borne alphavirus, causes debilitating febrile and arthritic disease and remains a persistent public health threat in tropical and subtropical regions, with no clinically approved antiviral drugs currently available, which underscores the urgent need for targeted and effective therapeutic interventions. Through high-throughput screening of an FDA-approved compound library, we identified retinoic acid (RA) as a broad-spectrum inhibitor of multiple arboviruses, exhibiting potent activity against CHIKV. Time-of-addition experiments, together with assays on viral binding, endocytosis, membrane fusion, replication and translation, were performed to determine the specific lifecycle stages inhibited by RA. Notably, RA exerts anti-CHIKV effects by selectively targeting eukaryotic translation initiation factor 4B (EIF4B), thereby disrupting the viral translation, as revealed by limited proteolysis-mass spectrometry (LiP-MS). And, our results demonstrated that RA administration exerted potent protective effects against CHIKV infection in vivo. Specifically, RA significantly reduced cerebral pathological damage, relieved clinical manifestations, and enhanced survival in a murine model of CHIKV-induced encephalitis, while also markedly attenuating footpad swelling and joint pathological alterations in a CHIKV-induced arthritis mouse model. Collectively, our findings highlight RA as a promising anti-CHIKV candidate targeting EIF4B, supporting its further development as a therapeutic agent against CHIKV infection. - Source: PubMed
Publication date: 2026/07/02
Chen YiboHe ZhiweiZhang KeQian XijingLiu YangangZheng XuZhao PingQi ZhongtianDing Cuiling - DEAD-box RNA helicases are central regulators of RNA metabolism, employing ATP-dependent mechanisms to remodel RNA structure and RNA-protein interactions, yet how helicase catalysis is coordinated with multi-subunit interactions between RNA and protein remains unresolved. Translation initiation helicase, eukaryotic initiation factor 4A (eIF4A), which acts as an intrinsically non-processive enzyme, is essential for unwinding structured mRNAs, relies on cofactors to achieve physiological activity. Here we uncover an unexpected RNA-helicase state of eIF4A, demonstrating that eIF4A forms nanometer-scale RNA-protein clusters (RPCs) of ~2-5 MDa in presence of its physiological cofactors eIF4B and eIF4G, RNA and ATP under near-physiological concentrations. Using a single molecule approach, we directly resolve the formation of discrete clusters that recruit multiple copies of proteins with RNA upon ATP addition and show that RPC formation correlates with helicase activity . Further, we find eIF4B as a key determinant of this multi-subunit assembly. Its intrinsically disordered regions (IDRs) together with structured RNA-recognition motifs (RRMs) drive multivalent RNA-dependent clustering, critical for efficient helicase activity. Disrupting eIF4B-RNA interactions through a targeted point mutation (F139A) in the RRM reduces both the cluster size and the helicase activity, further establishing a functional link between cluster formation and catalytic activity. Consistent with these findings, in-cell diffusion measurements reveal markedly slower diffusion of wild-type eIF4B compared with the RNA-binding-deficient mutant, indicative of RPC formation within the cellular environment. Together, our results reveal regulated helicase clustering as a previously unrecognized characteristic of the translation initiation machinery, linking ATP-dependent DEAD-box helicase activity to nanometer-scale RNA-protein clusters and translation initiation regulation. - Source: PubMed
Publication date: 2026/05/25
Shweta HimSokabe MasaakiVilla NancyFraser Christopher SGoldman Yale E