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

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.

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Resource Type: Diagram, Illustration, Journal article/Issue, Review
Audience Level: Undergraduate upper division 15-16, Graduate, Professional (degree program)

Author and Copyright


Authors and Editors: James R. Davie of Manitoba Institute of Cell Biology, University of Manitoba
Publisher: American Association for the Advancement of Science
Format: application/pdf, image/gif, image/jpeg, text/html
Copyright and other restrictions: Yes
Cost: Yes

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Collection:
STKE/Science Signaling


     
   

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