A fraction of the mRNA 5' cap-binding protein, eukaryotic initiation factor 4E, localizes to the nucleus

Proc Natl Acad Sci U S A. 1992 Oct 15;89(20):9612-6. doi: 10.1073/pnas.89.20.9612.

Abstract

The 5' cap structure m7GpppN (where N is any nucleotide) is a ubiquitous feature of cellular eukaryotic mRNAs. The cap is multifunctional as it is involved in translation, nucleocytoplasmic transport, splicing, and stabilization of mRNA against 5' exonucleolytic degradation. The cap binding protein, eukaryotic initiation factor 4E (eIF-4E), is a translation initiation factor that binds to the cap structure and is part of a complex (eIF-4F) that promotes mRNA binding to ribosomes. Overexpression of eIF-4E in fibroblasts results in cell transformation. To test the hypothesis that some of the biological effects of eIF-4E might be effected by a nuclear function, we determined the cellular distribution of eIF-4E. By means of indirect immunofluorescence experiments using polyclonal and monoclonal antibodies against eIF-4E as well as transfected epitope-tagged eIF-4E, we demonstrate that a fraction of eIF-4E localizes to the nucleus. These results suggest that eIF-4E is also involved in a nuclear function.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Blotting, Western
  • Cell Compartmentation
  • Cell Nucleus / metabolism*
  • Cells, Cultured
  • Chlorocebus aethiops
  • Epitopes
  • Eukaryotic Initiation Factor-4E
  • Fluorescent Antibody Technique
  • In Vitro Techniques
  • Molecular Sequence Data
  • Nuclear Proteins / metabolism*
  • Peptide Initiation Factors / metabolism*
  • RNA Caps / metabolism*

Substances

  • Epitopes
  • Eukaryotic Initiation Factor-4E
  • Nuclear Proteins
  • Peptide Initiation Factors
  • RNA Caps