An investigation into the splicing variants of human eIF4E isoforms and their distinct roles in stress

Abstract

The eukaryotic translation initiation factor 4E (eIF4E) binds to the 5' mRNA cap and plays a pivotal role in the control of cap-dependent translation initiation. The human eIF4E protein family comprises canonical eIF4E1 protein and two non-canonical isoforms eIF4E2 and eIF4E3. The different eIF4E isoforms have divergent biological roles ranging from translation initiation to mRNA repression and degradation. All of these isoforms can exist in multiple variants which arise as a result of alternative splicing. We will present summary of the known transcript variants coding for all three eIF4E isoforms extended by the analysis of alternate polyadenylation sites. Additionally, we will discuss the distinct behaviour of different protein variants of all three eIF4E isoforms during arsenite and heat stress.