Gene interactions and pathways from curated databases and text-mining
EMBO J 2006, PMID: 16541103

mTOR-dependent stimulation of the association of eIF4G and eIF3 by insulin.

Harris, Thurl E; Chi, An; Shabanowitz, Jeffrey; Hunt, Donald F; Rhoads, Robert E; Lawrence, John C

Insulin stimulates protein synthesis by increasing translation initiation. This response is mediated by mTOR and is believed to result from 4EBP1 phosphorylation, which allows eIF4E to bind eIF4G. Here, we present evidence that mTOR interacts directly with eIF3 and that mTOR controls the association of eIF3 and eIF4G. Activating mTOR signaling with insulin increased by as much as five-fold the amount of eIF4G bound to eIF3. This novel effect was blocked by rapamycin and other inhibitors of mTOR, and it required neither eIF4E binding to eIF4G nor eIF3 binding to the 40S ribosomal subunit. The increase in eIF4G associated with eIF3 occurred rapidly and at physiological concentrations of insulin. Moreover, the magnitude of the response was similar to the increase in eIF4E binding to eIF4G produced by insulin. Thus, increasing eIF4G association with eIF3 represents a potentially important mechanism by which insulin, as well as amino acids and growth factors that activate mTOR, stimulate translation.

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Text Mining Data

eIF3 → mTOR: " mTOR dependent stimulation of the association of eIF4G and eIF3 by insulin "

eIF4G → mTOR: " mTOR dependent stimulation of the association of eIF4G and eIF3 by insulin "

eIF3 — mTOR: " Here, we present evidence that mTOR interacts directly with eIF3 and that mTOR controls the association of eIF3 and eIF4G "

eIF4G — mTOR: " Here, we present evidence that mTOR interacts directly with eIF3 and that mTOR controls the association of eIF3 and eIF4G "

eIF3 ⊣ mTOR: " This novel effect was blocked by rapamycin and other inhibitors of mTOR , and it required neither eIF4E binding to eIF4G nor eIF3 binding to the 40S ribosomal subunit "

eIF4E ⊣ mTOR: " This novel effect was blocked by rapamycin and other inhibitors of mTOR , and it required neither eIF4E binding to eIF4G nor eIF3 binding to the 40S ribosomal subunit "

eIF4G ⊣ mTOR: " This novel effect was blocked by rapamycin and other inhibitors of mTOR , and it required neither eIF4E binding to eIF4G nor eIF3 binding to the 40S ribosomal subunit "

Manually curated Databases

  • IRef Biogrid Interaction: EIF4A1 — EIF4G1 (physical association, affinity chromatography technology)
  • IRef Biogrid Interaction: EIF3B — EIF4G1 (physical association, affinity chromatography technology)
  • IRef Biogrid Interaction: EIF3B — EIF3I (physical association, affinity chromatography technology)
  • IRef Biogrid Interaction: EIF3B — EIF4E (physical association, affinity chromatography technology)
  • IRef Biogrid Interaction: EIF3B — EIF4A1 (physical association, affinity chromatography technology)
  • IRef Biogrid Interaction: EIF3A — EIF4G1 (physical association, affinity chromatography technology)
  • IRef Biogrid Interaction: EIF3A — EIF3B (physical association, affinity chromatography technology)
  • IRef Biogrid Interaction: EIF4E — EIF4G1 (physical association, affinity chromatography technology)
  • IRef Biogrid Interaction: EIF3F — MTOR (physical association, affinity chromatography technology)
  • IRef Biogrid Interaction: EIF3F — MTOR (direct interaction, two hybrid)
  • IRef Biogrid Interaction: EIF3I — EIF4G1 (physical association, affinity chromatography technology)
  • IRef Hprd Interaction: EIF3B — EIF4G1 (in vivo)
  • IRef Hprd Interaction: EIF3A — EIF4G1 (in vivo)
  • IRef Hprd Interaction: EIF4E — EIF4G1 (in vivo)
  • IRef Hprd Interaction: EIF4E — EIF4G1 (in vitro)
  • IRef Hprd Interaction: EIF3F — MTOR (two hybrid)
  • IRef Hprd Interaction: EIF3F — MTOR (in vitro)
  • IRef Hprd Interaction: EIF3I — EIF4G1 (in vivo)
In total, 10 gene pairs are associated to this article in curated databases