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ICP0 inhibits BRCC3. 8 / 8
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"In this study, we revealed that HSV-1-encoded ICP0 can rapidly degrade host BRCC36 proteins, which results in downregulation of cellular IFNAR1 protein levels and subsequent inhibition of IFN-I antivi[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Taken together, HSV-1-encoded ICP0 downregulates host BRCC36 protein during the early stage of HSV-1 infection.Given that HSV-1-ICP0 is critical for BRCC36 downregulation, we next determined how ICP0 [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"We noticed that overexpression of Flag-ICP0 dramatically accelerated the degradation of endogenous BRCC36 proteins ( Fig. 3 B)."
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"Collectively, these findings suggest that HSV-1-encoded ICP0 could degrade BRCC36 protein in a ubiquitin-dependent manner.Based on the above findings, we speculated that ICP0 could induce ubiquitinati[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"For example, HSV-1 ICP0 protein was reported to degrade the host deubiquitinase BRCC36 and further downregulate IFN-I receptor IFNAR1 , and HSV-1 ICP27 protein was found to interfere with STAT-1 activation and hamper the downstream transcription of ISGs (interferon-stimulated genes) ."
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"Here, we found that HSV-1-encoded ICP0 degrades a host deubiquitinase BRCC36, which leads to inhibition of the strength of the IFN-IFNAR1 antiviral signaling.In summary, we demonstrated that HSV-1-enc[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"For example, ICP0 can disrupt promyelocytic leukemia nuclear bodies (PML-NBs) through the function of E3 Ub ligase, degrade speckled protein 100 (Sp100) in a RING-finger dependent manner, and degrade the host K63-linkage specific deubiquitinase BRCC36 to antagonize the type I interferon (IFN-1) antiviral response [9]."
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"HSV is particularly effective in this antagonism, with HSV ICP0 promoting degradation of the host deubiquitinase BRCC36, resulting in downregulation of IFNAR1 in a variety of human and mouse cell lines in vitro [140]."
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