Irf7 phosphorylation
WebNov 26, 2024 · Phosphorylation of MDA5 at Ser-828 by RIO kinase 3 inhibits the MDA5 multimer formation required for MAVS activation [25, 26]. ... (n = 4). b Mda5, c Irf1, d Irf3, e Irf7, f Irf8, and g Irf9. Assays are representative of at least three independent experiments showing similar results. WebIRF-7 plays an essential role in the induction of type I interferon in response viral infecton (6-8). Like IRF-3, IRF-7 is regulated at multiple serine phosphorylation sites near its …
Irf7 phosphorylation
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WebNov 7, 2016 · Phosphorylation of IRF7 is necessary for IFN- α signal transduction, followed by nuclear translocation and activation of type I IFN gene transcription [ 7, 8 ]. However, when the expression of type I IFN is dysregulated, adverse immunological effects may result. WebSep 1, 2024 · Irf3-/-Irf7-/-MEFs were a gift from Prof. Ping-hui Feng (University of Southern California, U.S.A.). Sendai virus (SeV) and GFP-containing vesicular stomatitis virus (VSV-GFP) were provided by Prof. Hongbin Shu (Wuhan University, China). ... Phosphorylation of Ser82 abolishes the promoter binding ability of IRF3. A&B. Immunoblot analysis of ...
WebIRF7, once induced, is present in the cytoplasm as an inactive protein that is also phosphorylated on specific C-terminal residues by TBK1 and/or possibly IKKε kinases ( Fitzgerald et al., 2003; Sharma et al., 2003 ). IRF7 has an important role in the regulation of IFNA genes other than A4. Websignaling pathways downstream of PRRs lead tothe phosphorylation of IFN regulatory factor 7 (IRF7) and IRF3, thus promoting their di-merization and translocation to the nucleus where they activate the transcription of type I IFN genes. IRF3 and IRF7 share some structural and functional similarities,
WebJul 25, 2024 · Here, we show that IRF3/IRF7 is transcriptionally active in a phase-separated state and reveal a mechanism for the role of IRF3/IRF7 LLPS-mediated ISRE binding, in which DBD deacetylation is... WebMay 25, 2007 · The IKK complex phosphorylates IκB, resulting in nuclear translocation of NF-κB, which induces expression of inflammatory cytokines. Stimulation of macrophages and DCs with LPS and dsRNA results in the activation of IRF3 and subsequent induction of IFN-β and IFN-inducible genes.
WebMar 6, 2024 · IRF7 is a key transcriptional factor involved in regulating IFN-α gene in lymphoid cells . Phosphorylation of IRF7 is necessary for IFN-α signal transduction, followed by nuclear translocation and activation of type I IFN gene transcription [7, 8]. However, when the expression of type I IFN is dysregulated, adverse immunological effects may ...
WebApr 2, 2024 · SAMHD1 also interacts with the inhibitor-κB kinase ε (IKKε) and IFN regulatory factor 7 (IRF7), leading to the suppression of the IFN-I induction pathway by reducing IKKε-mediated IRF7 phosphorylation. Interactions of endogenous SAMHD1 with NF-κB and IFN-I pathway proteins were validated in human monocytic cells and primary macrophages. dynamark graphics indianapolisWebIRF7 play a major role in the innate immune pathway, interacting with the Toll-like receptor (TLR) adaptor proteins MyD88 and Tirp/TRAM and functioning as an intermediate TLR4 … crystal steroidsWebMar 23, 2001 · IRF7 phosphorylation was blocked by staurosporine (Fig. 3 A, lane 4), a broad-spectrum kinase inhibitor previously shown to block phosphorylation of IRF1 in … crystal stevensWebThe study suggests that activation of IRF7 is more stringent than the activation of IRF3 (38). Mechanistically, IRF3 only requires phosphorylation of the 2S site for activation, whereas IRF7 ... dynamark graphics groupWebIRF-7 plays an essential role in the induction of type I interferon in response viral infection (6-8). Like IRF-3, IRF-7 is regulated at multiple serine phosphorylation sites near its … crystal stevens flourishWebA, kinetics of IRF7 phosphorylation. 293T cells transfected with 10 μg of an IRF7 expression construct were infected with NDV 12 h later, and nuclear extracts harvested at the … crystal stethoscope charmsWebIRF7 is synthesized as a latent protein and is posttranslationally modified by protein phosphorylation in infected cells. Phosphorylation required a carboxyl-terminal regulatory … crystal stevenson