{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,21]],"date-time":"2026-05-21T06:29:43Z","timestamp":1779344983384,"version":"3.51.4"},"reference-count":20,"publisher":"Wiley","issue":"1-2","license":[{"start":{"date-parts":[[2000,9,28]],"date-time":"2000-09-28T00:00:00Z","timestamp":970099200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["FEBS Letters"],"published-print":{"date-parts":[[2000,9,29]]},"abstract":"<jats:p>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\u2010 and stress\u2010activated protein kinase (MSK)1\u2212\/\u2212 and wild type cells in response to tetradecanoylphorbol acetate (TPA) and epidermal growth factor (EGF). TPA and EGF induced the phosphorylation of cyclic AMP\u2010responsive element binding protein (CREB) at Ser\u2010133 and ATF1 at Ser\u201063 in wild type cells and this was abolished by inhibition of the mitogen\u2010activated protein kinase cascade. In contrast, the TPA\u2010 and EGF\u2010induced phosphorylation of CREB\/ATF1 was barely detectable in MSK1\u2212\/\u2212 cells. However, basal and forskolin\u2010induced phosphorylation was similar, indicating that the MSK1 \u2018knockout\u2019 did not prevent CREB phosphorylation by cyclic AMP\u2010dependent protein kinase. 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