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

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 wit...

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Veröffentlicht in:FEBS letters 1999-09, Vol.457 (3), p.489-493
Hauptverfasser: Heesom, Kate J, Denton, Richard M
Format: Artikel
Sprache:eng
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Zusammenfassung: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.
ISSN:0014-5793
1873-3468
DOI:10.1016/S0014-5793(99)01094-7