IndraLab

"It has been resported that mouse USP18 interacts with IFNAR2 to negatively regulate type I IFN signaling [XREF_BIBR - XREF_BIBR]."

"USP18 's interaction with IFNAR2 also interfered with IFNAR2 's ability to recruit IFNAR1, hindering IFN I signaling [XREF_BIBR]."

"This isopeptidase-independent activity is mediated by the binding of USP18 to the intracellular domain of IFNAR2, which prevents the binding of JAK1."

"It was shown that USP18 directly interacted with IFN-α/β receptor 2 (IFNAR2) in human KT-1 cells, and competed for the binding of JAK1 to suppress type I IFN signaling [113,114] ."

"OTUD7A contributes to neuronal development [77,78] and USP18 regulates the immune response by binding to the interferon receptor IFNAR2 [82]."

"The IFN-mediated activation of the Jak-STAT pathway is tightly regulated by various cellular factors such as SOCS family members, USP18, the protein phosphatase 2A (PP2A), and protein inhibitors of STAT (PIAS).[ xref ] Along those lines, SOCS1 and SOCS3 transcriptional expression in hepatocytes remains detectable for only a short period of time upon alfa treatment indicating that by inhibiting Janus kinases both proteins are likely responsible for early termination of STAT activation.[ xref ] In addition, the sustained up-regulation of USP18 was associated with a long-lasting refractory state to IFN-α stimulation in hepatocytes and other primary human cells.[ xref ] The specific interaction of USP18 with IFNAR2 selectively affects IFN—induced signaling while having a marginal effect on other classes of IFNs, including type III IFNs."

"Mapping the STAT2 and USP18 binding to IFNAR2 by cell micropatterning of further deletions and mutations (XREF_SUPPLEMENTARY) confirmed aa 418-444 of IFNAR2 as a minimal interaction site for STAT2 and USP18."

"This effect is independent of the catalytic activity of USP18, which suggests that USP18 binding to IFNAR2 directly interferes with complex stabilization via the intracellular domains."

"The IFN-α signal-blocking activity of USP18 is mediated by the binding of USP18 to the intracellular domain of IFNAR2, which prevents the binding of JAK1 to IFNAR2 xref ."

"We assume that recruitment of USP18 to IFNAR2 via STAT2 promotes the otherwise weak interaction of USP18 with a membrane-proximal site of IFNAR2."

"Based on our previous report xref and the results presented above, USP18 interacts with both IFNAR2 and STAT2."

"Binding of STAT2 and USP18 to IFNAR2 is synergistic, in line with the previous observation that the STAT2-IFNAR2 interaction was strengthened by USP18 xref ."

"Taken together, our data suggest that USP18 simultaneously interacts with IFNAR2 via STAT2 in the membrane distal region and directly in the membrane-proximal region ( xref )."

"We next examined IFNAR2-independent interaction of STAT2 and USP18 in IFNAR2-deficient U5A cells by using cell micropatterning."

"More detailed analysis of the interaction dynamics of the STAT2–IFNAR2 interaction in the presence of USP18 by FRAP ( xref ) revealed a dissociation rate constant of 0.015 ± 0.005 s −1 ."

"These results established that USP18 independently interacts with IFNAR2 and STAT2."

"Mapping the STAT2 and USP18 binding to IFNAR2 by cell micropatterning of further deletions and mutations ( xref ) confirmed aa 418-444 of IFNAR2 as a minimal interaction site for STAT2 and USP18."

"The reported interactions between USP18 and IFNAR2 as well as STAT2 remain to be characterised biochemically and structurally."

"USP18 binds to IFNAR2 by competing with Jak1, thereby limits the activity of STATs and suppresses IFN response."

"Recently, it was also demonstrated that USP18 can directly interact with STAT2 to form a complex that inhibits IFN-I ligand binding to IFNAR2 ( xref , xref )."

"Even though type III IFN signaling requires JAK1, it is not affected by USP18 as USP18 specifically targets and binds IFNAR2 and not IFNLR ( xref )."

"In addition to its isopeptidase activity, USP18 negatively regulates type I and type III IFN signalling by blocking the IFNAR2 subunit of the interferon receptor ."

"In addition, independent of its enzymatic activity, USP18 can inhibit the type 1 interferon (IFN-1) signal transduction by binding the Interferon-alpha/beta receptor (IFNAR2) [18]."

"Even though type III IFN signaling requires JAK1, it is not affected by USP18 as USP18 specifically targets and binds IFNAR2 and not IFNLR."

"It is thus tempting to speculate that while the regulation of IFNAR2 signaling and ISG15 conjugation by USP18 are enzyme-independent and enzyme-dependent processes, respectively, they could still be coordinated by the same mechanism which involves the TAIL motif."

"USP18 was found to interact with the cytoplasmic domain of IFNAR2 and thus potentially down-regulate cell surface expression or binding affinity of IFNAR2."

"It has been resported that mouse USP18 interacts with IFNAR2 to negatively regulate type I IFN signaling [XREF_BIBR - XREF_BIBR]."

"USP18 's interaction with IFNAR2 also interfered with IFNAR2 's ability to recruit IFNAR1, hindering IFN I signaling [XREF_BIBR]."

"This isopeptidase-independent activity is mediated by the binding of USP18 to the intracellular domain of IFNAR2, which prevents the binding of JAK1."

"It was shown that USP18 directly interacted with IFN-α/β receptor 2 (IFNAR2) in human KT-1 cells, and competed for the binding of JAK1 to suppress type I IFN signaling [113,114] ."

"OTUD7A contributes to neuronal development [77,78] and USP18 regulates the immune response by binding to the interferon receptor IFNAR2 [82]."

"The IFN-mediated activation of the Jak-STAT pathway is tightly regulated by various cellular factors such as SOCS family members, USP18, the protein phosphatase 2A (PP2A), and protein inhibitors of STAT (PIAS).[ xref ] Along those lines, SOCS1 and SOCS3 transcriptional expression in hepatocytes remains detectable for only a short period of time upon alfa treatment indicating that by inhibiting Janus kinases both proteins are likely responsible for early termination of STAT activation.[ xref ] In addition, the sustained up-regulation of USP18 was associated with a long-lasting refractory state to IFN-α stimulation in hepatocytes and other primary human cells.[ xref ] The specific interaction of USP18 with IFNAR2 selectively affects IFN—induced signaling while having a marginal effect on other classes of IFNs, including type III IFNs."

"Mapping the STAT2 and USP18 binding to IFNAR2 by cell micropatterning of further deletions and mutations (XREF_SUPPLEMENTARY) confirmed aa 418-444 of IFNAR2 as a minimal interaction site for STAT2 and USP18."

"This effect is independent of the catalytic activity of USP18, which suggests that USP18 binding to IFNAR2 directly interferes with complex stabilization via the intracellular domains."

"The IFN-α signal-blocking activity of USP18 is mediated by the binding of USP18 to the intracellular domain of IFNAR2, which prevents the binding of JAK1 to IFNAR2 xref ."

"We assume that recruitment of USP18 to IFNAR2 via STAT2 promotes the otherwise weak interaction of USP18 with a membrane-proximal site of IFNAR2."

"Based on our previous report xref and the results presented above, USP18 interacts with both IFNAR2 and STAT2."

"Binding of STAT2 and USP18 to IFNAR2 is synergistic, in line with the previous observation that the STAT2-IFNAR2 interaction was strengthened by USP18 xref ."

"Taken together, our data suggest that USP18 simultaneously interacts with IFNAR2 via STAT2 in the membrane distal region and directly in the membrane-proximal region ( xref )."

"We next examined IFNAR2-independent interaction of STAT2 and USP18 in IFNAR2-deficient U5A cells by using cell micropatterning."

"More detailed analysis of the interaction dynamics of the STAT2–IFNAR2 interaction in the presence of USP18 by FRAP ( xref ) revealed a dissociation rate constant of 0.015 ± 0.005 s −1 ."

"These results established that USP18 independently interacts with IFNAR2 and STAT2."

"Mapping the STAT2 and USP18 binding to IFNAR2 by cell micropatterning of further deletions and mutations ( xref ) confirmed aa 418-444 of IFNAR2 as a minimal interaction site for STAT2 and USP18."

"The reported interactions between USP18 and IFNAR2 as well as STAT2 remain to be characterised biochemically and structurally."

"USP18 binds to IFNAR2 by competing with Jak1, thereby limits the activity of STATs and suppresses IFN response."

"Recently, it was also demonstrated that USP18 can directly interact with STAT2 to form a complex that inhibits IFN-I ligand binding to IFNAR2 ( xref , xref )."

"Even though type III IFN signaling requires JAK1, it is not affected by USP18 as USP18 specifically targets and binds IFNAR2 and not IFNLR ( xref )."

"Similarly, USP18, a ubiquitin-specific peptidase, is stimulated by JAK-STAT signaling and provides negative feedback to this pathway by binding IFNAR2, resulting in the promotion of viral replication [80]."