IndraLab

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USP15 deubiquitinates RIGI. 5 / 5
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"<span class="match term0">USP15</span> specifically removed lysine 63-linked polyubiquitin chains from <span class="match term1">RIG-I</span> among the essential components in <span class="match term1">RIG-I</span>-like receptor-dependent pathway"
26061460
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"Along a similar research line, our study showed that miR-26a serves as a potent positive regulator of IFN responses, highlighting the potential that miR-26a or its mimics can be further explored as a broad antiviral agent.On the other hand, in our study, we found that USP15 suppressed the type I interferon signaling by removing K63-linked of RIG-I ubiquitination, which is consistent with one previous research (24) but contrary with the results described in Pauli’s paper (37)."
38019020
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"For example, TNFAIP3, CYLD, USP3, USP4, USP15, USP25, and OTUD5 deubiquitinate key components of the IFN production pathway, including RIG-I, TRAF2, TRAF3, TRAF6, RIP1, and TRIF (reviewed in [93,94])."
38716888
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"USP15 specifically deubiquitinates RIG-I by direct physical association and does not interact with other signaling mediators like interferon-beta promoter stimulator 1 (IPS-1), TRAF3, and TBK1 in HEK293 cells."
33138315
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"Coimmunoprecipitation analysis showed that compared with control siRNA transfected cells, knockdown of USP15 substantially increased RIG-I polyubiquitination in WT ubiquitin and mutant Lys63 transfected cells (XREF_FIG)."
26061460