Under normal cellular conditions, eIF4F complex is limited as eIF4E is secluded from eIF4G by binding to hypophosphorylated eIF4E binding proteins (4E-BP). Stimulation of the phosphatidylinositol ...

A collaborative Project Team at The Institute of Cancer Research, London, and Astex Pharmaceuticals, Cambridge, identified a compound that can disrupt eIF4E’s interactions with a protein called eIF4G.

The eIF4 factors include mRNA 5′ cap-binding protein eIF4E, ATP-dependent RNA helicase eIF4A, and scaffold protein eIF4G, which anchors eIF4A and eIF4E. Another eIF4 factor, eIF4B, stimulates the RNA ...

mTOR activation also promotes the phosphorylation of protein translation initiation factor eIF4G at serine residue 1108 (P-eIF4G[ser1108]), as well as the dephosphorylation of eIF4E at serine residue ...

At the molecular level, IRE1α directly interacts with eIF4G and eIF3, 2 critical components of the translation initiation complex. We demonstrate that IRE1α facilitates the formation of the ...

Neurodegenerative diseases are commonly adult-onset conditions characterized by degeneration of specific neuronal populations. Familial forms are caused by mutations in single genes, but most ...

Disruption of either the entire eIF3 complex or specific targeting of these subunits affects mRNAs with long 5′-untranslated regions and whose translation is more dependent on eIF4A, eIF4B, and Ded1 ...

pombe homologue of eIF4G, Tif471. Our study demonstrates the impact of TOR‐dependent phospho‐regulation on the rate of protein synthesis and establishes a foundational resource for further ...

DEAD-box helicases mediate local RNA destabilization and unwinding in all processes involving RNA. Figure 1: The conformational cycle of the DEAD-box helicase core is linked to duplex destabilization ...

This complex prevents cap-dependent translation initiation by preventing eIF4G binding to eIF4E. Little is known about how the “decision” to activate translation is made, but our models suggests that ...

The team focused on a specific microexon located in a gene known as eIF4G, which is critical for protein synthesis in the cell. They found that this microexon is overwhelmingly excluded from eIF4G ...