The eIF4E-binding proteins are modifiers of cytoplasmic eIF4E relocalization during the heat shock response

Am J Physiol Cell Physiol. 2009 May;296(5):C1207-17. doi: 10.1152/ajpcell.00511.2008. Epub 2009 Feb 25.

Abstract

Stress granules (SGs) arise as a consequence of cellular stress, contain stalled translation preinitiation complexes, and are associated with cell survival during environmental insults. SGs are dynamic entities with proteins relocating into and out of them during stress. Among the repertoire of proteins present in SGs is eukaryotic initiation factor 4E (eIF4E), a translation factor required for cap-dependent translation and that regulates a rate-limiting step for protein synthesis. Herein, we demonstrate that localization of eIF4E to SGs is dependent on the presence of a family of repressor proteins, eIF4E-binding proteins (4E-BPs). Our results demonstrate that 4E-BPs regulate the SG localization of eIF4E.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adaptor Proteins, Signal Transducing / metabolism*
  • Antibiotics, Antineoplastic / pharmacology
  • Cell Cycle Proteins
  • Cell Line, Transformed
  • Cytoplasm / metabolism
  • Cytoplasmic Granules / metabolism
  • Eukaryotic Initiation Factor-4E / metabolism*
  • Eukaryotic Initiation Factors / metabolism*
  • Heat-Shock Response / physiology*
  • Humans
  • Oxidative Stress / physiology
  • Phosphoproteins / metabolism*
  • Protein Transport / drug effects
  • Protein Transport / physiology
  • Sirolimus / pharmacology

Substances

  • Adaptor Proteins, Signal Transducing
  • Antibiotics, Antineoplastic
  • Cell Cycle Proteins
  • EIF4EBP1 protein, human
  • EIF4EBP2 protein, human
  • Eukaryotic Initiation Factor-4E
  • Eukaryotic Initiation Factors
  • Phosphoproteins
  • Sirolimus