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[Cancer Research 64, 9076-9079, December 15, 2004]
© 2004 American Association for Cancer Research

Regular Articles

Mitogen- and Stress-Activated Protein Kinase 1 Activity and Histone H3 Phosphorylation in Oncogene-Transformed Mouse Fibroblasts

Bojan Drobic, Paula S. Espino and James R. Davie

Manitoba Institute of Cell Biology, Department of Biochemistry and Medical Genetics, University of Manitoba, Winnipeg, Manitoba, Canada

Activation of the Ras-Raf-mitogen-activated protein/extracellular signal-regulated kinase (ERK) kinase-ERK signal transduction pathway or the SAPK2/p38 pathway results in the activation of mitogen- and stress-activated protein kinase 1 (MSK1). This activation of MSK1 leads to a rapid phosphorylation of histone H3 at Ser10. Previously, we had demonstrated that Ser10 phosphorylated H3 was elevated in Ciras-3 (c-Ha-ras–transformed 10T1

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2) mouse fibroblasts and that H3 phosphatase activity was similar in Ciras-3 and 10T1

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2 cells. Here, we demonstrate that the activities of ERK and MSK1, but not p38, are elevated in Ciras-3 cells relative to these activities in the parental 10T1

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2 cells. Analyses of the subcellular distribution of MSK1 showed that the H3 kinase was similarly distributed in Ciras-3 and 10T1

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2 cells, with most MSK1 being present in the nucleus. In contrast to many other chromatin modifying enzymes, MSK1 was loosely bound in the nucleus and was not a component of the nuclear matrix. Our results provide evidence that oncogene-mediated activation of the Ras-mitogen-activated protein kinase signal transduction pathway elevates the activity of MSK1, resulting in the increased steady-state levels of phosphorylated H3, which may contribute to the chromatin decondensation and aberrant gene expression observed in these cells.




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Copyright © 2004 by the American Association for Cancer Research.