Phosphorylation of the translational repressor PHAS-I by the mammalian target of rapamycin.

The immunosuppressant rapamycin interferes with G1-phase progression in lymphoid and other cell types by inhibiting the function of the mammalian target of rapamycin (mTOR). mTOR was determined to be a terminal kinase in a signaling pathway that couples mitogenic stimulation to the phosphorylation of the eukaryotic initiation factor (eIF)-4E-binding protein, ...
PHAS-I. The rapamycin-sensitive protein kinase activity of mTOR was required for phosphorylation of PHAS-I in insulin-stimulated human embryonic kidney cells. mTOR phosphorylated PHAS-I on serine and threonine residues in vitro, and these modifications inhibited the binding of PHAS-I to eIF-4E. These studies define a role for mTOR in translational control and offer further insights into the mechanism whereby rapamycin inhibits G1-phase progression in mammalian cells.
Mesh Terms:
Adaptor Proteins, Signal Transducing, Androstadienes, Animals, Carrier Proteins, Cell Line, DNA-Binding Proteins, Eukaryotic Initiation Factor-4E, G1 Phase, Heat-Shock Proteins, Humans, Insulin, Peptide Initiation Factors, Phosphoproteins, Phosphorylation, Phosphotransferases (Alcohol Group Acceptor), Polyenes, Protein Kinases, Rats, Recombinant Proteins, Repressor Proteins, Signal Transduction, Sirolimus, TOR Serine-Threonine Kinases, Tacrolimus Binding Proteins, Transfection, Tumor Cells, Cultured
Science
Date: Jul. 04, 1997
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