Control of IRF-3 activation by phosphorylation.
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.
Yoneyama
Mitsutoshi
M
Department of Tumor Cell Biology, The Tokyo Metropolitan Institute of Medical Science, Tokyo 113-8613, Japan.
Suhara
Wakako
W
Fujita
Takashi
T
D000818:Animals; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D019281:Dimerization; D005544:Forecasting; D006801:Humans; D050838:Interferon Regulatory Factor-3; D009687:Nuclear Proteins / Q000737:chemistry / Q000378:metabolism; D010766:Phosphorylation; D011499:Protein Processing, Post-Translational; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism; D012330:RNA, Double-Stranded / Q000494:pharmacology; D015398:Signal Transduction; D015534:Trans-Activators / Q000737:chemistry / Q000378:metabolism; D014157:Transcription Factors / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D015533:Transcriptional Activation; D014777:Virus Diseases / Q000378:metabolism
D004268:DNA-Binding Proteins; C494232:IRF3 protein, human; D050838:Interferon Regulatory Factor-3; D009687:Nuclear Proteins; D012330:RNA, Double-Stranded; D015534:Trans-Activators; D014157:Transcription Factors; D017346:Protein Serine-Threonine Kinases