Control of IRF-3 activation by phosphorylation

J Interferon Cytokine Res. 2002 Jan;22(1):73-6. doi: 10.1089/107999002753452674.

Abstract

Interferon (IFN) regulatory factor-3 (IRF-3) is a unique member of the IRF family. Its transcriptional activity is regulated solely by posttranslational modifications. We review current knowledge of the mechanism of IRF-3 activation: signalling triggered by infections including viruses and bacteria, phosphorylation of IRF-3 on certain serine residues, homodimer formation, and active holocomplex formation with coactivator CBP/p300.

Publication types

  • Review

MeSH terms

  • Animals
  • DNA-Binding Proteins / chemistry
  • DNA-Binding Proteins / genetics
  • DNA-Binding Proteins / metabolism*
  • Dimerization
  • Forecasting
  • Humans
  • Interferon Regulatory Factor-3
  • Nuclear Proteins / chemistry
  • Nuclear Proteins / metabolism
  • Phosphorylation
  • Protein Processing, Post-Translational
  • Protein-Serine-Threonine Kinases / metabolism
  • RNA, Double-Stranded / pharmacology
  • Signal Transduction
  • Trans-Activators / chemistry
  • Trans-Activators / metabolism
  • Transcription Factors / chemistry
  • Transcription Factors / genetics
  • Transcription Factors / metabolism*
  • Transcriptional Activation
  • Virus Diseases / metabolism

Substances

  • DNA-Binding Proteins
  • IRF3 protein, human
  • Interferon Regulatory Factor-3
  • Nuclear Proteins
  • RNA, Double-Stranded
  • Trans-Activators
  • Transcription Factors
  • Protein-Serine-Threonine Kinases