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Sci STKE. 2003 Aug 12;2003(195):PE33.

MSK1 and MSK2 mediate mitogen- and stress-induced phosphorylation of histone H3: a controversy resolved.

Author information

1
Manitoba Institute of Cell Biology, University of Manitoba, 675 McDermot Avenue, Winnipeg, Manitoba, Canada, R3E 0V9. davie@cc.umanitoba.ca

Abstract

It is well established that mitogen- and stress-activated signal transduction pathways result in the rapid phosphorylation (Ser10 and Ser28) and acetylation of mammalian histone H3 associated with immediate-early genes. However, the prerequisite of H3 phosphorylation for the acetylation event and the identity of the mitogen-activated H3 kinase as RSK2 or MSK1 were controversial. A recent study with mouse embryonic fibroblasts lacking MSK1 and/or MSK2 demonstrated that MSK2 and MSK1 were the stimulus-induced H3 kinases and that neither of these enzyme activities was required for acetylation of H3 bound to immediate-early genes to occur.

PMID:
12915720
DOI:
10.1126/stke.2003.195.pe33
[Indexed for MEDLINE]

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