Anti-eIF3e antibody [EPR6878(2)]

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

EIF3e also known as eukaryotic translation initiation factor 3 subunit E is a critical component of the eIF3 complex. This protein has a mass of approximately 60 kDa and is expressed in a wide range of tissues. eIF3e plays a mechanical role in the translation initiation process facilitating the assembly of the pre-initiation complex by binding to the 40S ribosomal subunit and mRNA. It is essential for the correct positioning of mRNA in the ribosome enabling efficient start codon recognition.

Biological function summary

EIF3e participates in translation as part of the eIF3 complex which includes other subunits like eIF3a eIF3b and eIF3c. The complex facilitates ribosomal scanning and joining of the 60S ribosomal subunit promoting efficient protein synthesis. eIF3e specifically stabilizes the interaction of the initiation complex with mRNA ensuring accurate translation initiation. It is abundantly expressed in highly proliferative tissues reflecting its role in cell growth and division regulation.

Pathways

EIF3e plays a significant role in the mTOR signaling pathway and the Wnt signaling pathway. Both pathways regulate cell growth and proliferation which are important for development and tumorigenesis. eIF3e interacts with proteins like mTOR and beta-catenin that are integral to these pathways. It influences translation efficiency and has implications for protein synthesis regulation aligned with cellular growth cues.

Associated diseases and disorders

EIF3e has connections with cancer and viral infections. Aberrant expression and mutations of eIF3e occur in various cancers affecting normal translation control and promoting tumorigenesis. eIF3e also relates to viral pathogenesis as some viruses hijack the host's translation machinery involving eIF3e for viral protein synthesis. These interactions can involve proteins like p53 in cancer where eIF3e's dysregulation contributes to cell cycle alterations and oncogenesis.