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 |
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Hauptverfasser: | , |
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. |
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ISSN: | 0014-5793 1873-3468 |
DOI: | 10.1016/S0014-5793(99)01094-7 |