Dual utilization of an acceptor/donor splice site governs the alternative splicing of the IRF-3 gene.
Interferon regulatory factors constitute a family of transcriptional activators and repressors involved in a large number of vital cellular processes. Interferon regulatory factor-3 (IRF-3) has been implicated in virus and double-stranded RNA mediated induction of IFNbeta and RANTES, in DNA damage signaling, and in virus-induced apoptosis. With its critical role in these pathways, the activity of IRF-3 is tightly regulated in myriad ways. Here we describe novel regulation of IRF-3 at the level of RNA splicing. We show that an unprecedented dual utilization of a splice acceptor/donor site within the IRF-3 mRNA governs the production of two alternative splice isoforms.
Karpova
A Y
AY
Department of Pathology, Harvard Medical School, Boston, Massachusetts 02115, USA.
Howley
P M
PM
Ronco
L V
LV
D017398:Alternative Splicing; D000595:Amino Acid Sequence; D001483:Base Sequence; D002478:Cells, Cultured; D004268:DNA-Binding Proteins / Q000235:genetics*; D015698:Genomic Library; D006801:Humans; D050838:Interferon Regulatory Factor-3; D008969:Molecular Sequence Data; D009687:Nuclear Proteins / Q000378:metabolism; D010750:Phosphoproteins / Q000378:metabolism; D011485:Protein Binding; D016601:RNA-Binding Proteins / Q000378:metabolism; D000068103:Serine-Arginine Splicing Factors; D014157:Transcription Factors / Q000235:genetics*
D004268:DNA-Binding Proteins; C494232:IRF3 protein, human; D050838:Interferon Regulatory Factor-3; D009687:Nuclear Proteins; D010750:Phosphoproteins; D016601:RNA-Binding Proteins; D014157:Transcription Factors; D000068103:Serine-Arginine Splicing Factors