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eIF4E3 forms an active eIF4F complex during stresses (eIF4FS) targeting mTOR and re-programs the translatome.

Benjamin Weiss1, George Edward Allen1, Joachim Kloehn1

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The study reveals eukaryotic initiation factor 4E3 (eIF4E3) reprograms mRNA translation during cellular stress. This eIF4E3 complex promotes stress resistance and adaptation by selectively translating specific mRNAs.

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Area of Science:

  • Molecular Biology
  • Cellular Biology
  • Biochemistry

Background:

  • Eukaryotic initiation factors (eIF4E) regulate protein synthesis by binding mRNA 5' caps.
  • eIF4E1 controls global translation via the PI3K/AKT/mTOR pathway, while eIF4E2 regulates translation during hypoxia.
  • The precise role of eIF4E3 in translation and cellular response has been unclear.

Purpose of the Study:

  • To elucidate the function of eIF4E3 in cellular stress response.
  • To investigate the mechanism of eIF4E3 recruitment and its role in translation regulation.
  • To determine the impact of eIF4E3 on cellular metabolism and stress adaptation.

Main Methods:

  • Interaction studies to assess eIF4E3 binding partners.
  • Ribosome profiling (Ribo-seq) to analyze translation under stress conditions.
  • Generation of eIF4E3 knockout (KO) cells to study metabolic alterations.

Main Results:

  • eIF4E3 forms a translationally active complex (eIF4FS) during mTOR inhibition (Torin1 treatment).
  • The eIF4FS complex selectively translates mRNAs with specific 5' untranslated region (UTR) lengths.
  • eIF4E3 KO cells exhibit altered cellular metabolism upon Torin1 treatment, suggesting a role in stress adaptation.

Conclusions:

  • eIF4E3 functions as a distinct branch of the integrated stress response.
  • eIF4E3 re-programs the translatome to enhance cellular 'stress resistance' and adaptation.
  • eIF4E3 may possess 'moon-lighting' functions beyond canonical translation initiation.