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Dissociation of the eukaryotic initiation factor‐4E/4E‐BP1 complex involves phosphorylation of 4E‐BP1 by an mTOR‐associated kinase
Author(s) -
Heesom Kate J,
Denton Richard M
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)01094-7
Subject(s) - phosphorylation , pi3k/akt/mtor pathway , dissociation (chemistry) , eukaryotic initiation factor , kinase , microbiology and biotechnology , chemistry , protein kinase a , biology , biochemistry , signal transduction , gene , ribosome , rna
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.