Phosphorylation of eIF-4E positively regulates formation of the eIF-4F translation initiation complex following DNA damage

Ying Zhang, Yan Li, Da Qing Yang

Research output: Contribution to journalArticlepeer-review

11 Scopus citations

Abstract

The eukaryotic translation initiation factor 4E (eIF-4E) is essential for cap-dependent protein translation. However, the role of eIF-4E phosphorylation in protein translation is still unclear. In this study, the function of eIF-4E phosphorylation in the formation of the translational initiation complex eIF-4F following DNA damage was investigated. Our results show that etoposide treatment caused a rapid increase in eIF-4E phosphorylation. The addition of CGP57380, a specific inhibitor of the eIF-4E kinase Mnk, not only inhibited eIF-4E phosphorylation but also resulted in reduced interaction between eIF-4E and eIF-4G. Furthermore, neither the p38 MAPK inhibitor nor the ERK inhibitor caused significant inhibition in eIF-4E phosphorylation induced by etoposide. However, a JNK-specific inhibitor, SP600125, strongly suppressed etoposide-induced eIF-4E phosphorylation. Our results provide the first evidence indicating that phosphorylation of eIF-4E by Mnk, possibly mediated by JNK or JNK-like kinases, is critical for formation of the translational initiation complex eIF-4F following DNA damage.

Original languageEnglish (US)
Pages (from-to)54-59
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume367
Issue number1
DOIs
StatePublished - Feb 29 2008

Keywords

  • DNA damage
  • Translation initiation
  • eIF-4E phosphorylation
  • eIF-4F complex formation

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