Small-molecule inhibition of the interaction between the translation initiation factors eIF4E and eIF4G

Cell. 2007 Jan 26;128(2):257-67. doi: 10.1016/j.cell.2006.11.046.

Abstract

Assembly of the eIF4E/eIF4G complex has a central role in the regulation of gene expression at the level of translation initiation. This complex is regulated by the 4E-BPs, which compete with eIF4G for binding to eIF4E and which have tumor-suppressor activity. To pharmacologically mimic 4E-BP function we developed a high-throughput screening assay for identifying small-molecule inhibitors of the eIF4E/eIF4G interaction. The most potent compound identified, 4EGI-1, binds eIF4E, disrupts eIF4E/eIF4G association, and inhibits cap-dependent translation but not initiation factor-independent translation. While 4EGI-1 displaces eIF4G from eIF4E, it effectively enhances 4E-BP1 association both in vitro and in cells. 4EGI-1 inhibits cellular expression of oncogenic proteins encoded by weak mRNAs, exhibits activity against multiple cancer cell lines, and appears to have a preferential effect on transformed versus nontransformed cells. The identification of this compound provides a new tool for studying translational control and establishes a possible new strategy for cancer therapy.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Animals
  • Antineoplastic Agents / chemistry
  • Antineoplastic Agents / isolation & purification*
  • Antineoplastic Agents / pharmacology*
  • Cell Line, Transformed
  • Cell Line, Tumor
  • Cell Transformation, Neoplastic / drug effects*
  • Cell Transformation, Neoplastic / genetics
  • Cell Transformation, Neoplastic / metabolism
  • Drug Evaluation, Preclinical / methods
  • Eukaryotic Initiation Factor-4E / drug effects*
  • Eukaryotic Initiation Factor-4E / genetics
  • Eukaryotic Initiation Factor-4E / metabolism
  • Eukaryotic Initiation Factor-4G / drug effects*
  • Eukaryotic Initiation Factor-4G / genetics
  • Eukaryotic Initiation Factor-4G / metabolism
  • Feedback, Physiological / drug effects
  • Feedback, Physiological / physiology
  • Fluorescence Polarization Immunoassay / methods
  • Gene Expression Regulation, Neoplastic / drug effects*
  • Gene Expression Regulation, Neoplastic / genetics
  • Humans
  • Hydrazones
  • Jurkat Cells
  • Mice
  • Models, Molecular
  • Nitro Compounds / chemistry
  • Nitro Compounds / isolation & purification*
  • Nitro Compounds / pharmacology*
  • Oncogenes / drug effects
  • Oncogenes / genetics
  • Peptide Fragments / genetics
  • Peptide Fragments / metabolism
  • Peptide Fragments / pharmacology
  • Protein Binding / drug effects
  • Protein Binding / genetics
  • Protein Biosynthesis / drug effects
  • Protein Biosynthesis / genetics
  • RNA, Messenger / drug effects
  • RNA, Messenger / genetics
  • Thiazoles / chemistry
  • Thiazoles / isolation & purification*
  • Thiazoles / pharmacology*

Substances

  • 4EGI-1 compound
  • Antineoplastic Agents
  • Eukaryotic Initiation Factor-4E
  • Eukaryotic Initiation Factor-4G
  • Hydrazones
  • Nitro Compounds
  • Peptide Fragments
  • RNA, Messenger
  • Thiazoles