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USP19 inhibits TBK1. 6 / 6
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"Here, we demonstrate that USP19 (ubiquitin specific peptidase 19) interacts with and promotes TBK1 lysosomal degradation via chaperone-mediated autophagy (CMA)."
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"S4D), suggesting VANGL2-induced degradation of TBK1 to inhibit IFN-I signaling.Most literature showed that the degradation of TBK1 is relied on the proteasome, except for a few recent studies that indicated that USP19, NEDD4, and severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) nonstructural protein 13 (NSP13) could induce the autophagic degradation of TBK1 (7, 25, 26)."
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"Furthermore, USP19 deficiency in macrophages caused an elevation of TBK1 and the activation of the type-I interferon signaling pathway after vesicular stomatitis virus (VSV) infection."
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"Mechanistically, USP19 promoted the degradation of TBK1 in a lysosome-dependent manner, which serves an important role in the innate immune response against the virus [ 54 ]."
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"USP19 promotes the degradation of TBK1 through chaperone-mediated autophagy [ 36 ]."
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"51 It has been reported further that USP19 promotes TBK1 degradation through chaperone-mediated autophagy.52 Severe acute respiratory syndrome coronavirus 2 M protein also interacts with TBK1 and induces TBK1 degradation by K48-linked ubiquitination."
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