It takes a PHD to SUMO

Trends Biochem Sci. 2008 May;33(5):191-4. doi: 10.1016/j.tibs.2008.02.003. Epub 2008 Apr 9.

Abstract

PHD fingers and bromodomains are found in close proximity to each other in many chromatin-associated proteins and can functionally synergize. Recently, it has been demonstrated that the PHD finger of the KAP1 co-repressor functions as an E3 SUMO ligase for the adjacent bromodomain. This PHD-mediated SUMOylation stabilizes the association of the bromodomain with the chromatin modifiers SETDB1 and the nucleosome remodeling and deacetylation (NuRD) complex, thereby promoting establishment of the silent gene expression state.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • DNA-Binding Proteins / physiology*
  • Histone Deacetylases / metabolism
  • Histone-Lysine N-Methyltransferase
  • Humans
  • Mi-2 Nucleosome Remodeling and Deacetylase Complex
  • Models, Biological
  • Protein Methyltransferases / metabolism
  • Repressor Proteins / physiology*
  • Small Ubiquitin-Related Modifier Proteins / metabolism*
  • Tripartite Motif-Containing Protein 28
  • Ubiquitin-Protein Ligases / metabolism

Substances

  • DNA-Binding Proteins
  • Repressor Proteins
  • Small Ubiquitin-Related Modifier Proteins
  • Protein Methyltransferases
  • Histone-Lysine N-Methyltransferase
  • SETDB1 protein, human
  • TRIM28 protein, human
  • Tripartite Motif-Containing Protein 28
  • Ubiquitin-Protein Ligases
  • Histone Deacetylases
  • Mi-2 Nucleosome Remodeling and Deacetylase Complex