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USP25 inhibits STING1. 7 / 7
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"In addition, USP21 depletion contributed to the significant production of IFNs by activating the RIG-I or STING pathway, raising the possibility that USP21 inhibitors may enhance immune responses against virus infection (Fan et al., 2014; Chen et al., 2017a)."
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"The deubiquitinase USP21 can negatively regulate STING activity by removing K27- and K63 linked ubiquitin chains of STING [XREF_BIBR]."
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"Our data showed that overexpression of USP21 blocked translocation of STING from ER to a perinuclear microsome upon HSV-1 infection (XREF_FIG)."
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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]."
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"Our data showed that phosphorylation of USP21 by p38 promotes its binding to STING and inactivates STING in response to HSV-1 infection."
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"USP21 also negatively regulates STING function in promoting interferon production by deubiquitinating STING (98), a process negatively controlled by p38-MAPK (98)."
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"Hence, at late stages of viral infection, p38-mediated phosphorylation of USP21 (Ubiquitin Specific Peptidase 21), a deubiquitinating enzyme, inhibits STING."
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