Coupling 40S ribosome recruitment to modification of a cap-binding initiation factor by eIF3 subunit e

Derek Walsh*, Ian Mohr

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

25 Scopus citations

Abstract

40S ribosomes are loaded onto capped mRNAs via the multisubunit translation initiation factors eIF3 and eIF4F. While eIF4E is the eIF4F cap recognition component, the eIF4G subunit associates with 40S-bound eIF3. How this intricate process is coordinated remains poorly understood. Here, we identify an eIF3 subunit that regulates eIF4F modification and show that eIF3e is required for inducible eIF4E phosphorylation. Significantly, recruitment of the eIF4E kinase Mnk1 (MAPK signal-integrating kinase 1) to eIF4F depended on eIF3e, and eIF3e was sufficient to promote Mnk1-binding to eIF4G. This establishes a mechanism by which 40S ribosome loading imparts a phosphorylation mark on the cap-binding eIF4F complex that regulates selective mRNA translation and is synchronized by a specific eIF3 subunit.

Original languageEnglish (US)
Pages (from-to)835-840
Number of pages6
JournalGenes and Development
Volume28
Issue number8
DOIs
StatePublished - Apr 15 2014

Keywords

  • Mnk1
  • Ribosome recruitment
  • Translation initiation
  • eIF3
  • eIF4E phosphorylation

ASJC Scopus subject areas

  • Genetics
  • Developmental Biology

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