Abstract
Mouse embryonic stem (ES) cells homozygous for disruption of the MSK1 gene had no detectable MSK1 activity. However, their activators (extracellular signal related kinase (ERK)1/ERK2) were stimulated normally in mitogen- and stress-activated protein kinase (MSK)1-/- and wild type cells in response to tetradecanoylphorbol acetate (TPA) and epidermal growth factor (EGF). TPA and EGF induced the phosphorylation of cyclic AMP-responsive element binding protein (CREB) at Ser-133 and ATF1 at Ser-63 in wild type cells and this was abolished by inhibition of the mitogen-activated protein kinase cascade. In contrast, the TPA- and EGF-induced phosphorylation of CREB/ATF1 was barely detectable in MSK1-/- cells. However, basal and forskolin-induced phosphorylation was similar, indicating that the MSK1 'knockout' did not prevent CREB phosphorylation by cyclic AMP-dependent protein kinase. Thus MSK1 is required for CREB and ATF1 phosphorylation after mitogenic stimulation of ES cells.
| Original language | English |
|---|---|
| Pages (from-to) | 44-48 |
| Number of pages | 5 |
| Journal | FEBS Letters |
| Volume | 482 |
| Issue number | 1-2 |
| DOIs | |
| Publication status | Published - 29 Sept 2000 |
Keywords
- Animals
- Tetradecanoylphorbol Acetate
- Calcium-Calmodulin-Dependent Protein Kinases
- Recombinant Proteins
- Epidermal Growth Factor
- Chromosomes, Artificial, Bacterial
- Mice
- Cyclic AMP Response Element-Binding Protein
- Cloning, Molecular
- Mice, Knockout
- Mice, Inbred Strains
- Phosphorylation
- Ribosomal Protein S6 Kinases, 90-kDa
- Restriction Mapping
- Acetyltransferases
- Proteins
- Mitogen-Activated Protein Kinase 3
- Mitogen-Activated Protein Kinases
- Mitogen-Activated Protein Kinase 1
- Stem Cells
- Embryo, Mammalian