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PMID: 17502368,9121453,15864272 HuIFNAR1 also bound STAT1 and STAT2 via phospho-Tyr466 and phospho-Tyr48 when overexpressed in heterologous cells PMID: 17502368,9121453 Jak1, STAT1, and STAT2 may also be preassociated with IFNAR2 PMID: 17502368,16710296 Recently, a type I IFN-inducible cysteine protease, UBP43, was shown to interact directly with IFNAR2, blocking the interaction between Jak1 and the receptor PMID: 17502368,9121453 Jak1, STAT1, and STAT2 may also be preassociated with IFNAR2 PMID: 17502368,16311601 This may occur by binding a negative regulator such as SOCS-1 to inhibit JAK/STAT signaling PMID: 17502368,9121453 Jak1, STAT1, and STAT2 may also be preassociated with IFNAR2 PMID: 17502368,16311601 This may occur by binding a negative regulator such as SOCS-1 to inhibit JAK/STAT signaling PMID: 17502368,16311601,10022928,16710296 Thus, IFNARs also interact with a number of negative regulatory molecules, including SOCS-1 (suppressor of cytokine signaling), UBP43, and SHP , to limit the extent of signaling PMID: 17502368,16311601,10022928,16710296 Thus, IFNARs also interact with a number of negative regulatory molecules, including SOCS-1 (suppressor of cytokine signaling), UBP43, and SHP , to limit the extent of signaling PMID: 17502368,16311601,10022928,16710296 Thus, IFNARs also interact with a number of negative regulatory molecules, including SOCS-1 (suppressor of cytokine signaling), UBP43, and SHP , to limit the extent of signaling PMID: 17502368,16311601,10022928,16710296 Thus, IFNARs also interact with a number of negative regulatory molecules, including SOCS-1 (suppressor of cytokine signaling), UBP43, and SHP , to limit the extent of signaling PMID: 17502368,16311601,10022928,16710296 Thus, IFNARs also interact with a number of negative regulatory molecules, including SOCS-1 (suppressor of cytokine signaling), UBP43, and SHP , to limit the extent of signaling PMID: 17502368,16311601,10022928,16710296 Thus, IFNARs also interact with a number of negative regulatory molecules, including SOCS-1 (suppressor of cytokine signaling), UBP43, and SHP , to limit the extent of signaling PMID: 17502368,15337770 Residues within this region are also essential for the recruitment of E3 ubiquitin ligases and ubiquitination and degradation of the receptor PMID: 17502368, 15337770 Residues within this region are also essential for the recruitment of E3 ubiquitin ligases and ubiquitination and degradation of the receptor PMID: 17502368, 15337770 Residues within this region are also essential for the recruitment of E3 ubiquitin ligases and ubiquitination and degradation of the receptor PMID: 17502368,11154225 We have demonstrated in vitro that sIFNAR2a can bind IFN{alpha} or -beta and transduce a signal through IFNAR1 PMID: 17502368,11154225 We have demonstrated in vitro that sIFNAR2a can bind IFN{alpha} or -beta and transduce a signal through IFNAR1 PMID: 17502368 Figure 1B PMID: 17502368 conventional signaling occurs when IFN binds to IFNAR1 and tmIFNAR2c resulting in cross-phosphorylation of receptors and associated Janus kinases (Tyk2 and Jak1) PMID: 17502368 Figure 1B PMID: 17502368 conventional signaling occurs when IFN binds to IFNAR1 and tmIFNAR2c resulting in cross-phosphorylation of receptors and associated Janus kinases (Tyk2 and Jak1) PMID: 17502368 Figure 1B PMID: 17502368 conventional signaling occurs when IFN binds to IFNAR1 and tmIFNAR2c resulting in cross-phosphorylation of receptors and associated Janus kinases (Tyk2 and Jak1) PMID: 17502368 Figure 1B PMID: 17502368 conventional signaling occurs when IFN binds to IFNAR1 and tmIFNAR2c resulting in cross-phosphorylation of receptors and associated Janus kinases (Tyk2 and Jak1) PMID: 17502368 This provides docking sites on the receptor complex for STAT proteins. PMID: 17502368,9121453,15864272 HuIFNAR1 also bound STAT1 and STAT2 via phospho-Tyr466 and phospho-Tyr48 when overexpressed in heterologous cells PMID: 17502368,16311601 This may occur by binding a negative regulator such as SOCS-1 to inhibit JAK/STAT signaling PMID: 17502368 This provides docking sites on the receptor complex for STAT proteins. PMID: 17502368,16311601 This may occur by binding a negative regulator such as SOCS-1 to inhibit JAK/STAT signaling indirect PMID: 17502368 STAT proteins are in turn phosphorylated and form homo- and heterodimeric complexes, which dissociate from the receptor and then translocate to the nucleus and bind to an ISRE or GAS element within the promoters of interferon-regulated genes, leading to their transcription. indirect PMID: 17502368 STAT proteins are in turn phosphorylated and form homo- and heterodimeric complexes, which dissociate from the receptor and then translocate to the nucleus and bind to an ISRE or GAS element within the promoters of interferon-regulated genes, leading to their transcription. PMID: 17502368 STAT proteins are in turn phosphorylated and form homo- and heterodimeric complexes, which dissociate from the receptor and then translocate to the nucleus and bind to an ISRE or GAS element within the promoters of interferon-regulated genes, leading to their transcription. PMID: 17502368 STAT proteins are in turn phosphorylated and form homo- and heterodimeric complexes, which dissociate from the receptor and then translocate to the nucleus and bind to an ISRE or GAS element within the promoters of interferon-regulated genes, leading to their transcription. PMID: 17502368 STAT proteins are in turn phosphorylated and form homo- and heterodimeric complexes, which dissociate from the receptor and then translocate to the nucleus and bind to an ISRE or GAS element within the promoters of interferon-regulated genes, leading to their transcription. PMID: 17502368 STAT proteins are in turn phosphorylated and form homo- and heterodimeric complexes, which dissociate from the receptor and then translocate to the nucleus and bind to an ISRE or GAS element within the promoters of interferon-regulated genes, leading to their transcription. are in turn phosphorylated and form homo- and heterodimeric complexes, which dissociate from the receptor and then translocate to the nucleus and bind to an ISRE or GAS element within the promoters of interferon-regulated genes, leading to their transcription. PMID: 17502368 STAT proteins are in turn phosphorylated and form homo- and heterodimeric complexes, which dissociate from the receptor and then translocate to the nucleus and bind to an ISRE or GAS element within the promoters of interferon-regulated genes, leading to their transcription. are in turn phosphorylated and form homo- and heterodimeric complexes, which dissociate from the receptor and then translocate to the nucleus and bind to an ISRE or GAS element within the promoters of interferon-regulated genes, leading to their transcription. PMID: 17502368 STAT proteins are in turn phosphorylated and form homo- and heterodimeric complexes, which dissociate from the receptor and then translocate to the nucleus and bind to an ISRE or GAS element within the promoters of interferon-regulated genes, leading to their transcription. are in turn phosphorylated and form homo- and heterodimeric complexes, which dissociate from the receptor and then translocate to the nucleus and bind to an ISRE or GAS element within the promoters of interferon-regulated genes, leading to their transcription. PMID: 17502368 STAT proteins are in turn phosphorylated and form homo- and heterodimeric complexes, which dissociate from the receptor and then translocate to the nucleus and bind to an ISRE or GAS element within the promoters of interferon-regulated genes, leading to their transcription. are in turn phosphorylated and form homo- and heterodimeric complexes, which dissociate from the receptor and then translocate to the nucleus and bind to an ISRE or GAS element within the promoters of interferon-regulated genes, leading to their transcription. PMID: 17502368 STAT proteins are in turn phosphorylated and form homo- and heterodimeric complexes, which dissociate from the receptor and then translocate to the nucleus and bind to an ISRE or GAS element within the promoters of interferon-regulated genes, leading to their transcription. are in turn phosphorylated and form homo- and heterodimeric complexes, which dissociate from the receptor and then translocate to the nucleus and bind to an ISRE or GAS element within the promoters of interferon-regulated genes, leading to their transcription. PMID: 17502368 STAT proteins are in turn phosphorylated and form homo- and heterodimeric complexes, which dissociate from the receptor and then translocate to the nucleus and bind to an ISRE or GAS element within the promoters of interferon-regulated genes, leading to their transcription. are in turn phosphorylated and form homo- and heterodimeric complexes, which dissociate from the receptor and then translocate to the nucleus and bind to an ISRE or GAS element within the promoters of interferon-regulated genes, leading to their transcription. PMID: 17502368 STAT proteins are in turn phosphorylated and form homo- and heterodimeric complexes, which dissociate from the receptor and then translocate to the nucleus and bind to an ISRE or GAS element within the promoters of interferon-regulated genes, leading to their transcription. are in turn phosphorylated and form homo- and heterodimeric complexes, which dissociate from the receptor and then translocate to the nucleus and bind to an ISRE or GAS element within the promoters of interferon-regulated genes, leading to their transcription. PMID: 17502368 STAT proteins are in turn phosphorylated and form homo- and heterodimeric complexes, which dissociate from the receptor and then translocate to the nucleus and bind to an ISRE or GAS element within the promoters of interferon-regulated genes, leading to their transcription. are in turn phosphorylated and form homo- and heterodimeric complexes, which dissociate from the receptor and then translocate to the nucleus and bind to an ISRE or GAS element within the promoters of interferon-regulated genes, leading to their transcription. PMID: 17502368 STAT proteins are in turn phosphorylated and form homo- and heterodimeric complexes, which dissociate from the receptor and then translocate to the nucleus and bind to an ISRE or GAS element within the promoters of interferon-regulated genes, leading to their transcription. are in turn phosphorylated and form homo- and heterodimeric complexes, which dissociate from the receptor and then translocate to the nucleus and bind to an ISRE or GAS element within the promoters of interferon-regulated genes, leading to their transcription. indirect PMID: 17502368 STAT proteins are in turn phosphorylated and form homo- and heterodimeric complexes, which dissociate from the receptor and then translocate to the nucleus and bind to an ISRE or GAS element within the promoters of interferon-regulated genes, leading to their transcription. are in turn phosphorylated and form homo- and heterodimeric complexes, which dissociate from the receptor and then translocate to the nucleus and bind to an ISRE or GAS element within the promoters of interferon-regulated genes, leading to their transcription. indirect PMID: 17502368 STAT proteins are in turn phosphorylated and form homo- and heterodimeric complexes, which dissociate from the receptor and then translocate to the nucleus and bind to an ISRE or GAS element within the promoters of interferon-regulated genes, leading to their transcription. are in turn phosphorylated and form homo- and heterodimeric complexes, which dissociate from the receptor and then translocate to the nucleus and bind to an ISRE or GAS element within the promoters of interferon-regulated genes, leading to their transcription. indirect PMID: 17502368 STAT proteins are in turn phosphorylated and form homo- and heterodimeric complexes, which dissociate from the receptor and then translocate to the nucleus and bind to an ISRE or GAS element within the promoters of interferon-regulated genes, leading to their transcription. are in turn phosphorylated and form homo- and heterodimeric complexes, which dissociate from the receptor and then translocate to the nucleus and bind to an ISRE or GAS element within the promoters of interferon-regulated genes, leading to their transcription. PMID: 17502368,15449939,11125298,15312780 The binding site of IFN{alpha}2 on IFNAR1 has been predicted from site-directed mutagenesis and epitope mapping with an anti-IFNAR1-neutralizing antibody , albeit the latter may be inaccurate because of steric hindrances PMID: 17502368,12842042,15312780,9737924,10556041 Numerous studies have investigated the residues of IFNAR2 involved in ligand interactions with IFN{alpha}2 and IFNbeta PMID: 17502368,12842042,15312780,9737924,10556041 Numerous studies have investigated the residues of IFNAR2 involved in ligand interactions with IFN{alpha}2 and IFNbeta indirect indirect PMID: 17502368,15286706 In vitro studies demonstrate that a soluble IFNAR2 can also be generated by cleavage of transmembrane IFNAR2 by intramembrane proteases in response to IFNs and other stimuli, but there is no definitive in vivo evidence for this effect PMID: 17502368,15871661 Nevertheless, there is a precedent in the IL6 receptor system where the soluble IL6R{alpha} is generated both by alternative splicing and by cleavage by ADAM 10 and 17 proteases indirect PMID: 17502368,15871661 Nevertheless, there is a precedent in the IL6 receptor system where the soluble IL6R{alpha} is generated both by alternative splicing and by cleavage by ADAM 10 and 17 proteases