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Eukaryotic translation initiation factor 4B (EIF4B) is an RNA-binding protein critical for the initiation of protein synthesis in eukaryotic cells. As a cofactor for the DEAD-box RNA helicase eIF4A, EIF4B stimulates the unwinding of secondary structures in the 5′ untranslated regions (5′ UTRs) of mRNAs, facilitating ribosome scanning and start codon recognition[1][2][5]. EIF4B works in concert with other factors such as eIF4A, eIF4G, and RNA helicases like Ded1 to promote efficient translation, particularly for long mRNAs or those with highly structured 5′ UTRs[1]. In cancer and especially tumorigenic contexts, EIF4B is upregulated and binds the entire length of select mRNAs, modulating both translation and mRNA stability via interaction partners such as UPF1[2][3]. EIF4B is essential for cell cycle progression and proliferation, and its dysregulation contributes to tumorigenesis and resistance to cell cycle arrest[3]. Therapeutic targeting of EIF4B may indirectly impact tumor growth but raises concerns due to its central role in the control of global protein synthesis.
Inhibition of translation initiation, Indirect inhibition of eIF4B-dependent processes
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