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USP38 inhibits TBK1. 16 / 16
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"Furthermore, we found that USP38 expression reduced TBK1 protein, but not TBK1 mRNA, after VSV infection compared with 293T cells transfected with the empty vector (EV) ( Figures 4 H and S3 D)."
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"These results suggest that USP38 specifically degrades the active form (p-TBK1) of TBK1 after viral infection.It has been documented that TBK1 undergoes both K48-linked and K63-linked ubiquitination a[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Since the K48-linked ubiquitination of TBK1 is regulated by NLRP4, DTX4, or TRIP proteins ( Cui et al., 2012; Zhang et al., 2012 ), we first tested whether USP38 promotes TBK1 degradation by stabilizi[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"The results indicate that USP38 may promote the proteasomal degradation of p-TBK1 instead of the total TBK1."
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"Interestingly, we found that the USP38 (C545A/H857A) mutant failed to degrade TBK1, indicating that the deubiquitinating activity of USP38 is required to degrade TBK1 ( Figure 5 C)."
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"Amlexanox protects USP38 mediated cardiac remodeling, decreasing the protein expression of USP38-mediated TBK1/AKT-GSK3β/mTOR signaling pathway [158]."
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"USP38 deficiency abrogated the degradation of TBK1 and increased the production of type I IFN."
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"Similarly, USP38 negatively regulates IFN-I signaling by targeting the active form of TBK1 for degradation in vitro and in vivo (101)."
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"To determine the specificity of the USP38-mediated TBK1 degradation, we used other USP family members USP3 and USP13 as a control, and we found that USP38, but not USP3 or USP13, induced TBK1 degradat[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"However, the mRNA level of TBK1 remained unchanged ( Figure 4 A), suggesting that USP38 causes TBK1 protein degradation."
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"Several regulators, including DTX4, NLRP4, TRIM27, USP38, TRIP, and TRAF3IP3, can degrade TBK1 via the ubiquitin-proteasome pathway [37–41]."
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"To determine whether USP38 causes the degradation of other proteins, we performed a similar experiment and found that USP38 specifically degraded TBK1, but not IKKi, IKK-α, or IKK-β ( Figure 4 B)."
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"To determine whether USP38 degrades TBK1 through a ubiquitin-protease pathway, we performed experiments in the presence of the proteasome inhibitor MG-132 or 3-Methyladenine (3-MA), and we found that [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"USP38 strongly induced the degradation of the active form of TBK1 after viral infection."
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"Moreover, USP38 knockdown blocked the USP38-mediated degradation of TBK1 and restored ISRE-luc activity ( Figures 4 D and 4E)."
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"Murine USP38 (mUSP38) showed similar inhibitory function of human USP38 protein ( Figure S3 B), suggesting a conserved function of USP38 between mice and humans.To determine whether USP38 can mediate [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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