IndraLab

Statements

USP22 activates Ubiquitin. 7 / 7
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"Stability, USP22 can promote PD-L1 to remove the ubiquitin chain and prevent it from being degraded by the proteasome [13–16] ."
37769523
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"As suspected from its domain structure, USP22 is able to hydrolyze a ubiquitin linkage from histone H2B in vitro and endogenous USP22 contributes ubiquitin hydrolase activity to the hSAGA complex."
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"USP22 inhibits ubiquitin-mediated proteasomal degradation of SPI1."
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"Sevoflurane postconditioning upregulated USP22, which increased the protein content of lysine-specific demethylase 3A (KDM3a) in the promoter region of YAP1 by cutting the ubiquitin chains of the protein."
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"Interestingly, the human and fly SAGA complexes possess a module that houses ubiquitin hydrolase activity mediated by the USP22 (human) and Nonstop (fly) proteins."
19683498
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"37 It can be upregulated along with the poor prognosis by USP22 (ubiquitin‐specific peptidase 22) expression through MAPK1 pathway."
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"Another study also showed that USP22 interacted with PD-L1, enhancing its stability by removing ubiquitin and preventing its breakdown by the proteasome."
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