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 language | English |
|---|---|
| Pages (from-to) | 489-493 |
| Number of pages | 5 |
| Journal | FEBS Letters |
| Volume | 457 |
| Issue number | 3 |
| Publication status | Published - 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