Fig. 1

Overview of the canonical translation. During the initiation stage of translation, the 40S ribosomal subunit associates with various eIFs and the ternary complex to form the 43S PIC. The eIF4F complex recruits 43S PIC to the 5’ cap of mRNAs, forming the 48 S initiation complex. The recruitment process can be hindered by the eIF4E binding proteins (4EBPs), which disrupt the formation of the eIF4F complex. Once attached to mRNAs, the initiation complex scans the mRNA in the 5’ to 3’ direction to locate the start codon. Upon recognition of the start codon, initiation factors are released from the complex, and the 60 S large ribosomal subunit is recruited to assemble the 80 S ribosome. eIF2B catalyzes the reactivation of eIF2 by converting to its GTP-bound form, which can be inhibited by phosphorylated eIF2α. During translation elongation, eEF1A1 delivers cognate aminoacylated tRNA to the ribosome through base pairing between the codon and anticodon. With the assistance of eEF2, peptide elongation occurs as the ribosome translocates along the mRNA. Elongation continues until the ribosome reaches the stop codon. In eukaryotes, the termination of translation is mediated by the eRF1 and eRF3 complexes. These complexes play a role in the release of the nascent peptide, and subsequently, ABCE1 is recruited to the complex to facilitate the splitting of ribosomal subunits for recycling