Phosphorylation of the eukaryotic initiation factor 3f by cyclin-dependent kinase 11 during apoptosis.
eIF3f is a subunit of eukaryotic initiation factor 3 (eIF3). We previously showed that eIF3f is phosphorylated by cyclin dependent kinase 11 (CDK11(p46)) which is an important effector in apoptosis. Here, we identified a second eIF3f phosphorylation site (Thr119) by CDK11(p46) during apoptosis. We demonstrated that eIF3f is directly phosphorylated ... by CDK11(p46) in vivo. Phosphorylation of eIF3f plays an important role in regulating its function in translation and apoptosis. Phosphorylation of eIF3f enhances the association of eIF3f with the core eIF3 subunits during apoptosis. Our data suggested that eIF3f may inhibit translation by increasing the binding to the eIF3 complex during apoptosis.
Mesh Terms:
Amino Acid Sequence, Apoptosis, Binding Sites, Cyclin-Dependent Kinases, Eukaryotic Initiation Factor-3, Humans, Phosphorylation, Protein Biosynthesis, Protein Kinase Inhibitors, Protein Subunits, Tumor Cells, Cultured
Amino Acid Sequence, Apoptosis, Binding Sites, Cyclin-Dependent Kinases, Eukaryotic Initiation Factor-3, Humans, Phosphorylation, Protein Biosynthesis, Protein Kinase Inhibitors, Protein Subunits, Tumor Cells, Cultured
FEBS Lett.
Date: Mar. 18, 2009
PubMed ID: 19245811
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