Phosphorylation of the cap-binding protein eIF4E by the MAPK-activated protein kinase Mnk1

Biochem Pharmacol. 2000 Oct 15;60(8):1237-43. doi: 10.1016/s0006-2952(00)00429-9.

Abstract

The purpose of this review is to summarize recent experimental data describing the regulation of the phosphorylation of eIF4E, the cap-binding protein, by the MAPK-activated protein kinase Mnk1. Mnk1 does not interact directly with eIF4E, but uses a docking site in eIF4G, a partner of eIF4E. Consequently, control of eIF4E phosphorylation may not strictly depend on changes in Mnk1 activity. The possibility that integrity of the eIF4E/eIF4G/Mnk1 complex also impinges upon eIF4E phosphorylation is discussed.

Publication types

  • Review

MeSH terms

  • Cell Cycle / physiology
  • Eukaryotic Initiation Factor-4E
  • Eukaryotic Initiation Factor-4G
  • Humans
  • Intracellular Signaling Peptides and Proteins
  • Peptide Initiation Factors / metabolism*
  • Peptide Initiation Factors / physiology
  • Phosphorylation
  • Protein Binding
  • Protein-Serine-Threonine Kinases / metabolism*
  • RNA Cap-Binding Proteins
  • RNA-Binding Proteins / metabolism*

Substances

  • Eukaryotic Initiation Factor-4E
  • Eukaryotic Initiation Factor-4G
  • Intracellular Signaling Peptides and Proteins
  • Peptide Initiation Factors
  • RNA Cap-Binding Proteins
  • RNA-Binding Proteins
  • MKNK1 protein, human
  • Protein-Serine-Threonine Kinases