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USP38 binds TBK1. 9 / 9
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"Conversely, the K48-linked polyubiquitination level of TBK1 was obviously decreased after AdUSP38 transduced NRCMs (Figure 7B), These findings strongly indicate that USP38 interacts with and deubiquitinates TBK1 in hypertrophied cardiomyocytes."
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"Mechanistically, USP38 interacts with TANK-binding kinase 1 (TBK1) and removes K48-linked polyubiquitination of TBK1, stabilizing p-TBK1 and promoting the activation of its downstream mediators."
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"These results suggest that USP38, TRIP, and DTX4 may bind to TBK1 in an NLRP4-dependent manner."
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"To examine the interaction between USP38 and TBK1 under physiological conditions, we infected 293T cells, THP-1 cells, or PBMCs with VSV-EGFP, and we found that the interaction between USP38 and TBK1 [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"After viral infection, the interaction between USP38 and TBK1 was significantly increased in all three cell types ( Figures 3 D–3F)."
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"To substantiate these findings, we specifically knocked down NLRP4 and found that the interaction between USP38 and TBK1 was markedly attenuated ( Figure 6 F)."
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"Furthermore, we demonstrated that the dynamic interaction between USP38 and TBK1 was totally abrogated in NLRP4 small interfering RNA (siRNA)-treated THP-1 cells after viral infection ( Figure 6 G)."
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"As TBK1 is an upstream component of the Akt signaling pathway, and the TBK1-Akt signaling cascade is known to be significant in pathological cardiac remodeling4, we conducted a comprehensive analysis to explore the association between USP38 and TBK1."
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"co-immunoprecipitation suggests an interaction between USP38 and TBK1."
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