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ISG15 inhibits USP18. 14 / 14
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"However, by de-conjugating ISG15, the virus also creates free ISG15, which in turn may affect the immune response in two opposite pathways: free ISG15 negatively regulates IFN signaling in humans by binding non-catalytically to USP18, yet at the same time free ISG15 can be secreted from the cell and induce the IFN pathway of the neighboring cells."
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"In a follow-up report, Zhang et al. show that the absence of intracellular ISG15 in patients ' cells also prevents the accumulation of USP18, a potent negative regulator of type I IFN [XREF_BIBR]."
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"We further show that an absence of intracellular ISG15 in the patients ' cells prevents the accumulation of USP18 XREF_BIBR, XREF_BIBR, a potent negative regulator of IFN-alpha and beta signalling, resulting in the enhancement and amplification of IFN-alpha and beta responses."
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"Recently, human ISG15 deficiency was found to cause a decrease in USP18 accumulation and this was hypothesized to cause the loss of negative feedback of type I interferon signaling in these patients leading to auto-inflammation [XREF_BIBR]."
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"ISG15 is known to promote USP18-mediated inhibition of type I 437 IFN signaling by stabilizing USP18 activity and preventing its proteasomal degradation(Zhang et 438 al., 2015), underscoring the role of ISG15 as a negative regulator of type I IFN responses when 439 co-upregulated with USP18."
| DOI
eidos
"In turn , ISG15 prevents USP18 from being degraded by the proteasome ."
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"ISG15 prevents degradation of IFNAR’s negative regulator USP18, and as a result, type I IFN signaling is strongly enhanced in the absence of ISG15 (119, 120)."
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"This lack of intracellular free ISG15 prevents the accumulation of USP18, a known negative regulator of IFN-alpha and beta, resulting in enhanced IFN-alpha and beta immunity and autoinflammation, resembling Aicardi-Goutieres syndrome and spondyloenchondromatosis [XREF_BIBR, XREF_BIBR, XREF_BIBR]."
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"We therefore analysed the impact of ISG15 on SKP2 mediated USP18 degradation."
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"The authors also showed that intracellular ISG15 deficiency prevented ubiquitin specific peptidase 18 (USP18) accumulation."
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"Decreasing ISGylation by knockdown of the ISG15 E1 enzyme, Ube1L, in primary USP18(+/+) and USP18(−/−) hepatocytes led to increased MHV-3 replication."
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"By preventing USP18 degradation ISG15 stabilizes the interaction between IFNAR2 and USP18 (FIG."
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"In subsequent studies, engineered repression of USP18/UBP43 (ISG15 deconjugating enzyme) was shown to destabilize PML-RARα, reduce proliferation, and increase apoptosis in acute promyelocytic leukemia and lung cancer cell lines [169,170,171]."
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"In turn, ISG15 prevents USP18 from being degraded by the proteasome."
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