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FEBS Lett. 2000 Sep 29;482(1-2):44-8.

MSK1 is required for CREB phosphorylation in response to mitogens in mouse embryonic stem cells.

Author information

1
MRC Protein Phosphorylation Unit, Department of Biochemistry, University of Dundee, Dow Street, Dundee DD1 5EH, UK. j.s.c.arthur@dundee.ac.uk

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.

PMID:
11018520
DOI:
10.1016/s0014-5793(00)02031-7
[Indexed for MEDLINE]
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