Requirement of Rsk-2 for epidermal growth factor-activated phosphorylation of histone H3

Paolo Sassone-Corsi, Craig A. Mizzen, Peter Cheung, Claudia Crosio, Lucia Monaco, Sylvie Jacquot, André Hanauer, C. David Allis

Research output: Contribution to journalArticlepeer-review

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 pp90(rsk) family of kinases implicated in growth control, was required for epidermal growth factor (EGF)- stimulated phosphorylation of H3. RSK-2 mutations 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.

Original languageEnglish (US)
Pages (from-to)886-891
Number of pages6
JournalScience
Volume285
Issue number5429
DOIs
StatePublished - Aug 6 1999

ASJC Scopus subject areas

  • General

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