Anti-eIF4GII antibody - N-terminal

Supplementary info

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

Activity summary

The eukaryotic translation initiation factor 4GII (eIF4GII) also known as p97 plays an important role in the initiation of translation by acting as a central scaffold protein. With a molecular mass of approximately 160 kDa eIF4GII coordinates the assembly of the eIF4F translation initiation complex by interacting with other initiation factors and RNA. This protein is ubiquitously expressed across various tissues highlighting its fundamental role in protein synthesis.

Biological function summary

EIF4GII is integral to mRNA translation by facilitating the formation of the eIF4F complex which includes eIF4E eIF4A and itself. This complex binds to the 5' cap structure of mRNA an essential step for ribosome recruitment. eIF4GII performs functions important to translation regulation and cellular growth control influencing processes like cell proliferation and survival. Its activity links to mechanistic target mTOR signaling a pathway key to many cellular events.

Pathways

EIF4GII has significant involvement in the mTOR signaling pathway a major regulator of cell growth proliferation and protein synthesis. It operates alongside proteins such as eIF4E and eIF4A in this pathway facilitating the promotion of cap-dependent translation. eIF4GII also ties into the PI3K/AKT/mTOR axis influencing processes that control cell cycle progression and energy metabolism showing its role in the regulation of nutrient-sensitive signals.

Associated diseases and disorders

EIF4GII has implications in cancer and neurodegenerative diseases linked through its control of protein synthesis. Aberrant expression or regulation of eIF4GII can lead to uncontrolled cell proliferation and survival common in various cancers. In these contexts proteins like mTOR and eIF4E interact with eIF4GII in oncogenic pathways. In neurodegenerative disorders altered translation initiation involving eIF4GII contributes to the pathogenesis impacting neuronal survival and function due to defective protein synthesis control.