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USP21 inhibits STING1. 2 / 6
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"For example, NLRC3 activation in DCs attenuates their antigen presentation function through p38 MAPK activation, which also phosphorylates USP21 (ubiquitin-specific peptidase 21, a nuclear/cytoplasmic shuttling deubiquitinase) at Ser538 to inhibit STING activity by hydrolyzing its K27/63-linked polyubiquitin chain, which limits their ability to activate CD4 T cells and their polarization to pro-inflammatory Th1 and Th17 cells to prevent against autoinflammation and autoimmunity (Figure 3) [216,217,218]."

"In this study, we found that USP21 is an important deubiquitinating enzyme for STING and that it negatively regulates the DNA virus-induced production of type I interferons by hydrolyzing K27/63-linked polyubiquitin chain on STING. HSV-1 infection recruited USP21 to STING at late stage by p38-mediated phosphorylation of USP21 at Ser538. I"