Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2012 Dec 21;14(1):177–190. doi: 10.3390/ijms14010177

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© 2013 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland.

This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).

PMC Copyright notice

Translational functions of the eIF3 and eIF4F complexes and inhibition by the 4E-BPs. The eIF4F complex is composed of eIF4E, eIF4G and eIF4A. The interaction between eIF4F (bound to the cap structure via its eIF4E subunit) and eIF3 (bound to the 40S ribosomal particle) complexes permits ribosome docking at the 5′ extremity of capped mRNAs. The melting of mRNA structures by the RNA helicase eIF4A facilitates ribosome binding to mRNA, and the interaction between eIF4G and PABP results in mRNA circularization, a feature that is believed to enhance mRNA translation. eIF4G recruits the eIF4E kinases MNK1 and MNK2. In stressed cells, the dephosphorylation of 4E-BPs disrupts the eIF4E-eIF4G interaction, inhibiting general cap-dependent translation (left arrow). However the translation of selected mRNAs is still possible due to the existence of either uORFs or IRESes (right arrow). See text for details.