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Sci. STKE, 12 August 2003
Vol. 2003, Issue 195, p. pe33
[DOI: 10.1126/scisignal.1952003pe33]

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MSK1 and MSK2 Mediate Mitogen- and Stress-Induced Phosphorylation of Histone H3: A Controversy Resolved

James R. Davie*

Manitoba Institute of Cell Biology, University of Manitoba, 675 McDermot Avenue, Winnipeg, Manitoba, Canada, R3E 0V9

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.

*Contact information. E-mail, davie{at}cc.umanitoba.ca

Citation: J. R. Davie, MSK1 and MSK2 Mediate Mitogen- and Stress-Induced Phosphorylation of Histone H3: A Controversy Resolved. Sci. STKE 2003, pe33 (2003).

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THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Inducible Covalent Posttranslational Modification of Histone H3.
A. M. Bode and Z. Dong (2005)
Sci. STKE 2005, re4
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