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Requirement of Rsk-2 for Epidermal Growth Factor-Activated Phosphorylation of Histone H3

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Science  06 Aug 1999:
Vol. 285, Issue 5429, pp. 886-891
DOI: 10.1126/science.285.5429.886

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Abstract

During the immediate-early response of mammalian cells to mitogens, histone H3 is rapidly and transiently phosphorylated by one or more unidentified kinases. Rsk-2, a member of the pp90rsk family of kinases implicated in growth control, was required for epidermal growth factor (EGF)–stimulated phosphorylation of H3. RSK-2mutations in humans are linked to Coffin-Lowry syndrome (CLS). Fibroblasts derived from a CLS patient failed to exhibit EGF-stimulated phosphorylation of H3, although H3 was phosphorylated during mitosis. Introduction of the wild-type RSK-2 gene restored EGF-stimulated phosphorylation of H3 in CLS cells. In addition, disruption of the RSK-2 gene by homologous recombination in murine embryonic stem cells abolished EGF-stimulated phosphorylation of H3. H3 appears to be a direct or indirect target of Rsk-2, suggesting that chromatin remodeling might contribute to mitogen-activated protein kinase–regulated gene expression.

  • * To whom correspondence should be addressed. E-mail: paolosc{at}igbmc.u-strasbg.fr; allis{at}virginia.edu

  • These authors contributed equally to this work. The contributions of the Sassone-Corsi and Allis labs were equal.

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