eIF-2 kinases: regulators of general and gene-specific translation initiation

Trends Biochem Sci. 1994 Nov;19(11):491-6. doi: 10.1016/0968-0004(94)90136-8.

Abstract

Phosphorylation of eukaryotic initiation factor-2 (eIF-2) is an important mechanism regulating general translation initiation. Two mammalian eIF-2 kinases, the double-stranded-RNA-dependent kinase (PKR) and heme-regulated inhibitor kinase (HRI), have been characterized by sequencing, revealing shared sequence and structural features distinct from other eukaryotic protein kinases. Recent work in yeast has shown that a third related kinase, GCN2, also phosphorylates the regulated site in eIF-2. However, unlike the mammalian kinases, this kinase regulates gene-specific translation. Current models are presented for the regulation of each eIF-2 kinase, and the molecular basis for how this general form of regulation is adapted to control expression of a single species of messenger RNA is discussed.

Publication types

  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Molecular Sequence Data
  • Peptide Chain Initiation, Translational / physiology*
  • Phosphorylation
  • Protein Biosynthesis*
  • Protein-Serine-Threonine Kinases
  • eIF-2 Kinase

Substances

  • Protein-Serine-Threonine Kinases
  • eIF-2 Kinase