IndraLab

Statements


USP18 leads to the dephosphorylation of STAT1. 8 / 8
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"Silencing of USP18 by siRNA was later shown to prolong STAT1 phosphorylation and enhance ISG expression, resulting in a synergistic antiviral effect on HCV treated with IFN [XREF_BIBR]."

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"In line with this result, expression of aa 36-372, but not aa 51-372, of USP18 inhibited STAT1 phosphorylation upon IFNalpha treatment (XREF_SUPPLEMENTARY)."

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"Our results showed that USP18 overexpression significantly inhibited IFNT-induced phosphorylation of STAT1 protein."

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"Specifically, IFNλs but not type I IFNs activate JAK2 affecting immune cell functions in a way type I IFNs cannot do [ 19 , 20 ], USP18 acts as a negative regulator of IFNλ signaling and inhibits the [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"Unphosphorylated STAT1 and STAT2 are also upregulated by USP18 knockdown, suggesting their possible implication in IFNalpha induced chemokine expression."

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"The authors have demonstrated that: (i) infection of iMphs with HIV-1 induces USP18; (ii) depletion of USP18 with CRISPR/Cas9 increases iMph reactivity to IFNI, the phosphorylation of STAT1 and STAT2, the expression of IFN-stimulated genes and ultimately results in a significant restriction of HIV replication in iMphs."

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"USP18 acts to prevent JAK1 from binding to IFN-I receptor and hence arrests phosphorylation of STAT1 and STAT2, essential components of the transcription factor complex that induces ISGs."

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"USP18 silencing restored phosphorylation of STAT1 after IFN-alpha treatment, and forced expression of WT USP18 or enzymatically inactive C64S USP18 mutant blocked phosphorylation of STAT1."