EIF3d and eIF4G2 mediate an alternative mechanism of cap-dependent but eIF4E-independent translation initiation.

ABSTRACT: Initiation of translation for the majority of eukaryotic mRNAs is mediated by a 5' cap structure to which the eukaryotic initiation factor 4E (eIF4E) binds. Inhibition of the activity of eIF4E by 4EBP-1 does not prevent the translation of a number of cellular capped mRNAs, indicative of the existence of previously unexplored mechanisms for the translation of these capped mRNAs without the requirement of eIF4E. eIF4G2, also known as death-associated protein 5 (DAP5), a homolog of eIFGI that lacks the eIF4E binding domain, utilizes eIF3d (a subunit of eIF3) to promote the translation of a subset of these mRNAs. Using fluorescence anisotropy-based equilibrium binding studies, we provide the first quantitative evidence of the recruitment of eIF3d as well as eIF3d and eIFG2 complexes to a subse

SUBMITTER: Quartey JNK 

PROVIDER: S-EPMC11968281 | biostudies-literature | 2025 Apr

REPOSITORIES: biostudies-literature