Eukaryotic translation initiation factor 6 (EIF6)

Eukaryotic translation initiation factor 6 (EIF6) is a highly conserved protein that plays a critical role in both ribosome biogenesis and the regulation of translation in eukaryotic cells[1][3][4]. EIF6 binds specifically to the 60S ribosomal subunit, functioning as an anti-association factor that prevents premature assembly of the 40S and 60S ribosomal subunits into the 80S ribosome[1][2][6]. In the nucleolus, EIF6 is essential for the maturation and export of the 60S pre-ribosomal subunit, whereas in the cytoplasm, it must dissociate from 60S before the ribosome can initiate translation[1][2][3]. The activity of EIF6 is regulated through post-translational modifications such as phosphorylation, with kinases like PKC involved in controlling its release from 60S, a process essential to translation initiation[7]. EIF6 is indispensable for cell growth, highly expressed in proliferative tissues, and required for tissue-specific growth and oncogene-driven transformation[1][3][4]. Disruption of EIF6 levels unbalances ribosome production and translation, with potential implications in cancer biology and metabolic regulation[4][5]. No direct drugs or small-molecule inhibitors are currently established for EIF6, and its essential cellular role limits its targetability, but its critical position in translation control and tumorigenesis has brought it increasing attention as a candidate for cancer research.

Other names

Eukaryotic initiation factor 6eIF6Integrin beta-4 binding proteinITGB4BPp27BBPCABb(2)gcnOK/SW-cl.27B4 integrin interactor