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

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-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.

Pubmed ID: 10436156


  • Sassone-Corsi P
  • Mizzen CA
  • Cheung P
  • Crosio C
  • Monaco L
  • Jacquot S
  • Hanauer A
  • Allis CD


Science (New York, N.Y.)

Publication Data

August 6, 1999

Associated Grants

  • Agency: NIGMS NIH HHS, Id: GM40922

Mesh Terms

  • 3T3 Cells
  • Abnormalities, Multiple
  • Animals
  • Calcium-Calmodulin-Dependent Protein Kinases
  • Cell Line, Transformed
  • Cell Nucleus
  • Cells, Cultured
  • Epidermal Growth Factor
  • Gene Expression Regulation
  • Gene Targeting
  • Histones
  • Humans
  • Mice
  • Mitosis
  • Mutation
  • Phosphorylation
  • Ribosomal Protein S6 Kinases
  • Signal Transduction
  • Stem Cells
  • Syndrome