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

    Research output: Contribution to journal › Article (Academic Journal) › peer-review

    88 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 Sept 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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