IRF3
GeneName
IRF3
Summary
IRF3, also known as interferon regulatory factor 3, is a 47 kDa transcription factor that plays a pivotal role in the antiviral innate immune response. It is predominantly expressed in the cytoplasm and translocates to the nucleus upon activation. IRF3 is involved in the regulation of genes that produce type I interferons and other cytokines, which are crucial for the immune response to viral infections. It binds to specific DNA sequences to activate or repress transcription, thereby influencing various immune processes including the cellular response to viruses and the regulation of inflammatory responses. IRF3 is also implicated in the cGAS/STING and TLR signalling pathways, which are essential for detecting viral pathogens and initiating immune responses.
Importance
IRF3 is relevant to: - The regulation of antiviral responses through its role in type I interferon production, which is essential for controlling viral infections. - The modulation of inflammatory responses, impacting conditions such as autoimmune diseases and chronic inflammation. - The interplay between apoptosis and immune responses, particularly in macrophage function and the resolution of inflammation. - The understanding of signalling pathways like cGAS/STING and TLR, which are critical for innate immunity and therapeutic targets in infectious diseases.
Top Products
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Abcam Product Citation Summary
The data indicates that IRF3 is a significant target in studies related to apoptosis, Type I IFN signalling, and immune responses. The use of various Abcam antibodies in both mouse and human cell lines highlights the relevance of IRF3 in different biological contexts, including responses to treatments and signalling pathways.
Abcam Product Citation Table
Function
Key transcriptional regulator of type I interferon (IFN)-dependent immune responses which plays a critical role in the innate immune response against DNA and RNA viruses (PubMed:22394562, PubMed:24049179, PubMed:25636800, PubMed:27302953, PubMed:31340999, PubMed:36603579, PubMed:8524823). Regulates the transcription of type I IFN genes (IFN-alpha and IFN-beta) and IFN-stimulated genes (ISG) by binding to an interferon-stimulated response element (ISRE) in their promoters (PubMed:11846977, PubMed:16846591, PubMed:16979567, PubMed:20049431, PubMed:32972995, PubMed:36603579, PubMed:8524823). Acts as a more potent activator of the IFN-beta (IFNB) gene than the IFN-alpha (IFNA) gene and plays a critical role in both the early and late phases of the IFNA/B gene induction (PubMed:16846591, PubMed:16979567, PubMed:20049431, PubMed:36603579). Found in an inactive form in the cytoplasm of uninfected cells and following viral infection, double-stranded RNA (dsRNA), or toll-like receptor (TLR) signaling, is phosphorylated by IKBKE and TBK1 kinases (PubMed:22394562, PubMed:25636800, PubMed:27302953, PubMed:36603579). This induces a conformational change, leading to its dimerization and nuclear localization and association with CREB binding protein (CREBBP) to form dsRNA-activated factor 1 (DRAF1), a complex which activates the transcription of the type I IFN and ISG genes (PubMed:16154084, PubMed:27302953, PubMed:33440148, PubMed:36603579). Can activate distinct gene expression programs in macrophages and can induce significant apoptosis in primary macrophages (PubMed:16846591). In response to Sendai virus infection, is recruited by TOMM70:HSP90AA1 to mitochondrion and forms an apoptosis complex TOMM70IRF3:BAX inducing apoptosis (PubMed:25609812). Key transcription factor regulating the IFN response during SARS-CoV-2 infection (PubMed:33440148).
Involvement in disease
Encephalopathy, acute, infection-induced, 7, herpes-specific
IIAE7
A rare complication of human herpesvirus 1 (HHV-1) infection, occurring in only a small minority of HHV-1 infected individuals. It is characterized by hemorrhagic necrosis of parts of the temporal and frontal lobes. Onset is over several days and involves fever, headache, seizures, stupor, and often coma, frequently with a fatal outcome.
None
Disease susceptibility is associated with variants affecting the gene represented in this entry.
Post-translational modifications
Constitutively phosphorylated on many Ser/Thr residues (PubMed:22394562, PubMed:23478265, PubMed:23746807). Activated following phosphorylation by TBK1 and IKBKE (PubMed:23478265, PubMed:23746807, PubMed:25636800, PubMed:36603579). Innate adapter proteins, such as MAVS, STING1 or TICAM1, are first activated by viral RNA, cytosolic DNA, and bacterial lipopolysaccharide (LPS), respectively, leading to activation of the kinases TBK1 and IKBKE (PubMed:25636800). These kinases then phosphorylate the adapter proteins on the pLxIS motif, leading to recruitment of IRF3, thereby licensing IRF3 for phosphorylation by TBK1 (PubMed:25636800). Phosphorylation at Ser-386 is followed by pyrophosphorylation at the same residue, promoting phosphorylation at Ser-396 (PubMed:36603579). Phosphorylated IRF3 dissociates from the adapter proteins, dimerizes, and then enters the nucleus to induce IFNs (PubMed:25636800, PubMed:36603579).
Pyrophosphorylated by UAP1 following phosphorylation at Ser-386 by TBK1 (PubMed:36603579). Pyrophosphorylation promotes subsequent phosphorylation at Ser-396, leading to homodimerization of IRF3 (PubMed:36603579).
Acetylation at Lys-366 by KAT8 inhibits recruimtent to promoters and transcription factor activity. Acetylation by KAT8 is promoted by phosphorylation at Ser-396.
Ubiquitinated; ubiquitination involves RBCK1 leading to proteasomal degradation (PubMed:18711448). Polyubiquitinated; ubiquitination involves TRIM21 leading to proteasomal degradation (PubMed:18641315). Ubiquitinated by UBE3C, leading to its degradation (PubMed:21167755).
ISGylated by HERC5 resulting in sustained IRF3 activation and in the inhibition of IRF3 ubiquitination by disrupting PIN1 binding. The phosphorylation state of IRF3 does not alter ISGylation.
Proteolytically cleaved by apoptotic caspases during apoptosis, leading to its inactivation (PubMed:30878284). Cleavage by CASP3 during virus-induced apoptosis inactivates it, preventing cytokine overproduction (PubMed:30878284).
(Microbial infection) ISGylated. ISGylation is cleaved and removed by SARS-COV-2 nsp3 which attenuates type I interferon responses.
(Microbial infection) Phosphorylation and subsequent activation of IRF3 is inhibited by vaccinia virus protein E3.
(Microbial infection) Phosphorylated by herpes simplex virus 1/HHV-1 US3 at Ser-175 to prevent IRF3 activation.
Sequence Similarities
Belongs to the IRF family.
Tissue Specificity
Expressed constitutively in a variety of tissues.
Cellular localization
- Cytoplasm
- Nucleus
- Mitochondrion
- Shuttles between cytoplasmic and nuclear compartments, with export being the prevailing effect (PubMed:10805757, PubMed:35922005). When activated, IRF3 interaction with CREBBP prevents its export to the cytoplasm (PubMed:10805757). Recruited to mitochondria via TOMM70:HSP90AA1 upon Sendai virus infection (PubMed:25609812).
Alternative names
Interferon regulatory factor 3, IRF-3, IRF3
Database links
swissprot:Q14653 entrezGene:3661 omim:603734
Other research areas
- Epigenetics