IndraLab

Statements

USP22 binds KPNA2. 3 / 3
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"Results from endogenous immunoprecipitation assays suggest that KPNA2 interacted with USP22 constitutively but interacted with IRF3 or pIRF3 in THP-1 cells in a manner dependent on viral infection ( xref )."
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"In our study, we found that knockout of USP22 impaired virus-triggered nuclear translocation of p65 and induction of p65-target genes such as Tnf and Il6 , which was restored by reconstitution of KPNA2, suggesting a role of the USP22–KPNA2 axis in NF-κB activation after viral infection (data not shown)."
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"In contrast, mutation of USP22 NLS (USP22-RR/AA) did not affect its association with KPNA2 ( xref ), suggesting that USP22 interacts with KPNA2 independently of its NLS."
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