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Phosphorylation of the proto-oncogene product eukaryotic initiation factor 4E is a common cellular response to tumor

M W Marino1, L J Feld, E A Jaffe

  • 1Memorial Sloan-Kettering Cancer Center, New York, New York.

Insights

Tumor necrosis factor-alpha (TNF) triggers rapid phosphorylation of eukaryotic initiation factor 4E, a key mRNA cap-binding protein. This early event impacts cellular translation and is crucial for TNF

Area of Science:

  • Molecular Biology
  • Cellular Biology
  • Biochemistry

Background:

  • mRNA translation initiation is a critical regulatory step controlled by the phosphorylation of initiation factors.
  • Tumor necrosis factor-alpha (TNF) is a cytokine with diverse cellular functions, many of which are initiated early in cellular responses.

Purpose of the Study:

  • To investigate the effect of TNF on the phosphorylation of mRNA translation initiation factors.
  • To identify the specific protein targeted by TNF-induced phosphorylation during translation initiation.

Main Methods:

  • Utilized various cell types as in vitro models for TNF action.
  • Purified, sequenced, and identified the specific mRNA cap-binding protein affected by TNF.
  • Analyzed the phosphorylation status of the identified protein in response to TNF stimulation.

Main Results:

  • TNF rapidly stimulates the phosphorylation of an mRNA cap-binding protein in multiple cell types.
  • The phosphorylated protein was identified as eukaryotic initiation factor 4E (eIF4E), a proto-oncogene product.
  • Phosphorylation of eIF4E is an early and common event in diverse TNF-mediated cellular actions.

Conclusions:

  • TNF-induced phosphorylation of eukaryotic initiation factor 4E is a significant early event in cellular responses.
  • This post-translational modification of a key translation factor highlights a mechanism by which TNF regulates protein synthesis.
  • The findings provide insights into the molecular pathways linking TNF signaling to cellular processes.

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