Article
Multiple mechanisms control phosphorylation of PHAS-I in five (S/T)P sites that govern translational repression.
Molecular and cellular biology - 1 May 2000
Mothe-Satney I, Yang D, Fadden P, Haystead T A, Lawrence J C
Abstract excerpt
Control of the translational repressor, PHAS-I, was investigated by expressing proteins with Ser/Thr --> Ala mutations in the five (S/T)P phosphorylation sites. Results of experiments with HEK293 cells reveal at least three levels of control. At one extreme is nonregulated phosphorylation, exemplified by constitutive phosphorylation of Ser82. At an intermediate level, amino acids and insulin stimulate the...
Topics
- Amino Acids
- Carrier Proteins
- Eukaryotic Initiation Factor-4E
- Insulin
- Mutation
- Peptide Initiation Factors
- Phosphoproteins
- Phosphorylation
- Protein Biosynthesis
- RNA Caps
- Repressor Proteins
- Serine
- Sirolimus
- Threonine