RING finger protein 4 (RNF4) derepresses gene expression from DNA methylation

J Biol Chem. 2014 Dec 5;289(49):33808-13. doi: 10.1074/jbc.C114.611558. Epub 2014 Oct 29.

Abstract

RNF4 is an E3 ubiquitin ligase originally identified as a transcription co-activator. The mechanism by which RNF4 promotes transcription remains unclear. In this study, I found that RNF4 antagonizes transcriptional repression mediated by DNA methylation. RNF4 does not promote DNA demethylation, but mediates the ubiquitination of MeCP2, a methyl-CpG-binding domain (MBD) protein. Removal of MeCP2 from gene promoters activates transcription. This study thus not only uncovers how RNF4 functions as a transcription activator, but also reveals the mechanism by which MeCP2 protein stability is regulated.

Keywords: DNA Methylation; Methyl CpG-binding Protein 2 (MeCP2); Protein Turnover; RING Finger Protein 4 (RNF4); Transcription; Ubiquitylation (Ubiquitination).

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • DNA Methylation
  • Epigenesis, Genetic*
  • Genes, Reporter
  • Green Fluorescent Proteins / genetics
  • Green Fluorescent Proteins / metabolism
  • HEK293 Cells
  • Humans
  • Methyl-CpG-Binding Protein 2 / genetics*
  • Methyl-CpG-Binding Protein 2 / metabolism
  • Nuclear Proteins / genetics*
  • Nuclear Proteins / metabolism
  • Protein Stability
  • Signal Transduction
  • Transcription Factors / genetics*
  • Transcription Factors / metabolism
  • Transcription, Genetic*
  • Ubiquitination

Substances

  • MECP2 protein, human
  • Methyl-CpG-Binding Protein 2
  • Nuclear Proteins
  • RNF4 protein, human
  • Transcription Factors
  • Green Fluorescent Proteins