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[Cancer Research 62, 75-78, January 1, 2002]
© 2002 American Association for Cancer Research

Biochemistry and Biophysics

Ser-10 Phosphorylation of Histone H3 and Immediate Early Gene Expression in Oncogene-transformed Mouse Fibroblasts1

Ileana S. Strelkov and James R. Davie2

Manitoba Institute of Cell Biology, Winnipeg, Manitoba, R3E 0V9 Canada

Stimulation of the Ras-mitogen-activated protein kinase (MAPK) pathway by growth factors, phorbol esters, and oncoproteins results in the phosphorylation of histone H3. Rsk-2 and MSK1 have been reported to be H3 kinases activated by the Ras-MAPK signal transduction pathway. In this study, we used inhibitors of Rsk-2 and MSK1 to decide which of these kinases was responsible for the 12-O-tetradecanoylphorbol-13-acetate (TPA)-induced phosphorylation of H3 in 10T1/2 and Ciras-3 (H-ras-transformed 10T1/2) mouse fibroblasts. These studies demonstrated that MSK1, but not Rsk-2, was the H3 kinase activated in these cells. Furthermore, assays with Rsk-2 showed that this kinase phosphorylates H2B but not H3 in vitro. H89, a potent MSK1 inhibitor, prevented TPA induction of H3 phosphorylation and diminished the TPA-induced expression of the c-fos and urokinase plasminogen activator genes. We propose that persistent activation of the Ras-MAPK pathway and MSK1 resulting in the elevation of phosphorylated H3 levels may contribute to the aberrant gene expression observed in the oncogene-transformed cells.




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Copyright © 2002 by the American Association for Cancer Research.