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USP15 binds TRIM25. 27 / 29
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"In the RLR-mediated signaling pathway, E6 forms a three-molecule complex with TRIM25 and USP15, which triggers the K48-linked ubiquitination and proteasomal degradation of TRIM25, attenuates the TRIM25-mediated K63-linked ubiquitination of RIG-I."
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"USP15 bound to TRIM25 specifically late during infection, removing Lys48-linked ubiquitin chains from TRIM25 and thus stabilizing it [81]."
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No evidence text available
24399297
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No evidence text available
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"In contrast, USP15 substantially interacted with TRIM25 at later time points during SeV infection."
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"Moreover, a recent study identified the USP15–TRIM25 dyad as a pivotal regulatory complex in proinflammatory and antiviral responses [29]."
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"USP15 binds to TRIM25 in viral infections, detaching the K48 linked ubiquitin chains assembled by LUBAC on TRIM25, thereby stabilizing the TRIM25 protein levels and promoting a sustained antiviral response."
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"The E6 oncoproteins of several HPVs (both low-risk and high-risk) form a complex with TRIM25 and USP15, which ultimately prevents the K63-linked ubiquitination of the RIG-I CARDs."
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"Torre et al. validated a functional interaction of a complex of USP15 with TRIM25 in neuroinflammation by showing ECM resistance in double heterozygous Usp15 L749R/+ Trim25 +/− mice."
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"USP15 binds to TRIM25 in viral infections, detaching the K48-linked ubiquitin chains assembled by LUBAC on TRIM25, thereby stabilizing the TRIM25 protein levels and promoting a sustained antiviral response (Figure 3)."
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"For instance, USP15 interacts with and deubiquitinates TRIM25 when it is ubiquitinated by the E3 complex LUBAC."
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"USP15 binds to TRIM25 in viral infections, detaching the K48-linked ubiquitin chains assembled by LUBAC on TRIM25, thereby stabilizing the TRIM25 protein levels and promoting a sustained antiviral response (Figure xref )."
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"Furthermore, whereas our results showed that USP15 efficiently interacted with TRIM25 specifically in infected cells, USP4 constitutively interacts with RIG-I."
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"Instead, coimmunoprecipitation and confocal microscopy studies indicated that USP15 efficiently bound to TRIM25 in virus infected cells, whereas, in contrast, a TRIM25-USP15 interaction was barely detectable in un infected cells."
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"Consistently, there was increased binding of USP15 to TRIM25 in infected primary normal human lung fibroblasts (NHLFs), whereas the interaction was minimal in uninfected cells (XREF_SUPPLEMENTARY)."
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No evidence text available
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"Furthermore, HPV E6 protein forms a ternary complex with USP15 and TRIM25, resulting in the inhibition of immune surveillance and antiviral responses, thereby exhibiting a direct involvement in immune system regulation [ xref ]."
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"USP15 bound to TRIM25 specifically late during infection, removing Lys48-linked ubiquitin chains from TRIM25 and thus stabilizing it [81]."
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No evidence text available
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"USP15 physically interacts with TRIM25."
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"We first confirmed the physical interaction between TRIM25 and USP15 with coimmunoprecipitation experiments."
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"USP15 bound to TRIM25 specifically late during infection, removing Lys48 linked ubiquitin chains from TRIM25 and thus stabilizing it XREF_BIBR."
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"USP15 bound to TRIM25 specifically late during infection, removing Lys48-linked ubiquitin chains from TRIM25 and thus stabilizing it xref ."
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"USP15 binds to TRIM25 in viral infections, detaching the K48-linked ubiquitin chains assembled by LUBAC on TRIM25, thereby stabilizing the TRIM25 protein levels and promoting a sustained antiviral response (Figure 3)."
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"The E6 oncoprotein of HPV16 interacts with TRIM25 and USP15, promoting K48-linked ubiquitination of TRIM25 and suppressing TRIM25-mediated K63-linked ubiquitination of RIG-I to evade the host antiviral response ( xref )."
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"The E6 oncoprotein of HPV16 interacts with TRIM25 and USP15, promoting K48-linked ubiquitination of TRIM25 and suppressing TRIM25-mediated K63-linked ubiquitination of RIG-I to evade the host antiviral response (Chiang et al., 2018a)."
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"Interestingly, it has been shown that HPV16 E6, but not E7, forms a complex with TRIM25 and its regulator ubiquitin carboxyl-terminal hydrolase 15 (USP15), inducing TRIM25 degradation [ xref ]."
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