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Updated: Jan 8, 2026

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eIF5 has GDI activity necessary for translational control by eIF2 phosphorylation.

Martin D Jennings1, Graham D Pavitt

  • 1Faculty of Life Sciences, University of Manchester, Michael Smith Building, Oxford Road, Manchester M13 9PT, UK.

Nature
|May 21, 2010
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Summary

Eukaryotic translation initiation factor 5 (eIF5) acts as a GDP dissociation inhibitor (GDI) to recycle eIF2, and regulates translation during stress by inhibiting eIF2B.

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Eukaryotic translation initiation factor 2 (eIF2) delivers initiator tRNA to the ribosome.
  • Phosphorylation of eIF2 (eIF2αP) is crucial for regulating protein synthesis.
  • eIF5 acts as a GTPase accelerating protein (GAP) in translation initiation.

Purpose of the Study:

  • To investigate novel regulatory roles of eIF5 in translation initiation.
  • To elucidate the function of eIF5 in the recycling of eIF2.
  • To define eIF5's role in the regulation of eIF2αP.

Main Methods:

  • Biochemical assays to assess GDP binding to eIF2.
  • Site-directed mutagenesis to identify key residues in eIF5.
  • Analysis of the eIF2αP regulatory complex.

Main Results:

  • eIF5 stabilizes GDP binding to eIF2, acting as a GDP dissociation inhibitor (GDI).
  • This GDI activity is separate from its GAP function.
  • eIF5 is essential for the inhibitory complex regulating the guanine-nucleotide exchange factor eIF2B.

Conclusions:

  • eIF5 possesses dual functions: GAP and GDI.
  • eIF5 plays a critical role in the recycling of eIF2.
  • eIF5 is a key regulator of translational control, particularly under stress conditions.