Modulation of 14-3-3 interaction with phosphorylated histone H3 by combinatorial modification patterns

Stefan Winter, Wolfgang Fischle, Christian Seiser*

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

41 Scopus citations


Post-translational modifications of histones are determining factors in the global and local regulation of genome activity. Phosphorylation of histone H3 is globally associated with mitotic chromatin compaction but occurs in a much more restricted manner during interphase transcriptional regulation of a limited subset of genes. In the course of gene regulation, serine 10 phosphorylation at histone H3 is targeted to a very small fraction of nucleosomes that is highly susceptible to additional acetylation events. Recently, we and others have identified 14-3-3 as a binding protein that recognizes both phosphorylated serine 10 and phosphorylated serine 28 on histone H3. In vitro, the affinity of 14-3-3 for phosphoserine 10 is weak but becomes significantly increased by additional acetylation of either lysine 9 or lysine 14 on the same histone tail. In contrast, the histone H3S28 site matches elements of 14-3-3 high affinity consensus motifs. This region mediates an initial stronger interaction that is less susceptible to modulation by "auxiliary" modifications. Here we discuss the binding of 14-3-3 proteins to histone H3 in detail and putative biological implications of these interactions.

Original languageEnglish (US)
Pages (from-to)1336-1342
Number of pages7
JournalCell Cycle
Issue number10
StatePublished - May 15 2008
Externally publishedYes


  • Epigenetics
  • Histone code
  • Methylation
  • Phosphoacetylation
  • Transcription

ASJC Scopus subject areas

  • Molecular Biology
  • Developmental Biology
  • Cell Biology


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