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Interferon regulatory factors (IRF) are proteins which regulate transcription of interferons (see regulation of gene expression). [1] Interferon regulatory factors contain a conserved N-terminal region of about 120 amino acids, which folds into a structure that binds specifically to the IRF-element (IRF-E) motifs, which is located upstream of the interferon genes. [2]
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IRF3 is a member of the interferon regulatory transcription factor (IRF) family. [5] IRF3 was originally discovered as a homolog of IRF1 and IRF2.IRF3 has been further characterized and shown to contain several functional domains including a nuclear export signal, a DNA-binding domain, a C-terminal IRF association domain and several regulatory phosphorylation sites. [6]
IRF5 is a direct transducer to interferon signaling and is activated via phosphorylation. [11] The IRF family can also initiate the JAK/STAT signaling pathway by binding to transmembrane receptors that activate JAK. [12] IRFs, IFNs, and the JAK/STAT signaling pathway work together to fight viral infections in mammals through specific signals. [13]
[27] [28] Reducing IFN-α activity may prevent signaling via STAT1, STAT2, or IRF9 (as with JEV infection) or through the JAK-STAT pathway (as with DEN-2 infection). [26] Several poxviruses encode soluble IFN receptor homologs—like the B18R protein of the vaccinia virus—that bind to and prevent IFN interacting with its cellular receptor ...
Interferon regulatory factor 1 was the first member of the interferon regulatory transcription factor (IRF) family identified. Initially described as a transcription factor able to activate expression of the cytokine Interferon beta, [6] IRF-1 was subsequently shown to function as a transcriptional activator or repressor of a variety of target genes.
The upstream signaling pathway is triggered by the binding of a signaling molecule, a ligand, to a receiving molecule, a receptor. Receptors and ligands exist in many different forms, and only recognize/bond to particular molecules. Upstream extracellular signaling transduce a variety of intracellular cascades. [1]
IFN-τ binds to IFNAR cell membrane receptor and induces dimerization of its subunits, IFNAR1 and IFNAR2, which leads to activation of canonical and noncanonical signaling pathways. The canonical pathway involves Janus kinase-signal transducer and activator of transcription-interferon regulatory factor ( JAK - STAT - IRF ) signaling.