Dissociation of the eukaryotic initiation factor-4E/4E-BP1 complex involves phosphorylation of 4E-BP1 by an mTOR-associated kinase

KJ Heesom*, RM Denton

*Corresponding author for this work

Research output: Contribution to journalArticle (Academic Journal)peer-review

79 Citations (Scopus)

Abstract

mTOR immunoprecipitates contain two 4E-BP1 protein kinase activities. One appears to be due to mTOR itself and results in the phosphorylation of 4E-BP1 on residues T-36 and T-45, as shown previously by others. The other is a kinase which can be separated from mTOR and which phosphorylates 4E-BP1 within a peptide(s) containing residues S-64 and T-69 This phosphorylation, which occurs predominantly on S-64, results in the dissociation of 4E-BP1 from eIF-4E, (C) 1999 Federation of European Biochemical Societies.

Original languageEnglish
Pages (from-to)489-493
Number of pages5
JournalFEBS Letters
Volume457
Issue number3
Publication statusPublished - 3 Sep 1999

Keywords

  • mTOR
  • 4E-BP1
  • phosphorylation
  • mRNA translation initiation
  • insulin
  • ACTIVATED PROTEIN-KINASE
  • RAT FAT-CELLS
  • MAMMALIAN TARGET
  • PHAS-I
  • TRANSLATIONAL REGULATOR
  • 4E-BINDING PROTEIN-1
  • ADIPOSE-TISSUE
  • INSULIN
  • RAPAMYCIN
  • SITES

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