IndraLab

Statements

USP22 is ubiquitinated. 13 / 13
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"Interestingly, we also observed Morusin caused conformational changes in the active pocket residues 255–262 after MD-50 ns, indicating that Morusin may inhibit USP22 ubiquitination activity through al[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Further analysis revealed that IFN-γ treatment promotes USP22 ubiquitination and degradation ( xref )."
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"Loss of AKT-mediated phosphorylation markedly increased USP22 ubiquitination and abolished EPI-induced inhibitory efficacy ( xref )."
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"However, of those four DUBs, only USP22 substantially decreased KDM1A ubiquitination ( xref )."
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"Treatment with topotecan had no significant effect on USP22 mRNA levels (Figure xref ), but facilitated the ubiquitination of USP22 (Figure  xref )."
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"Stimulation with EPI markedly reduced USP22 ubiquitination levels ( xref ), supporting our speculation that EPI protects USP22 from ubiquitination-mediated degradation."
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"(1) Inhibition of SLC7A11 expression: the ubiquitination of ubiquitin specific peptidase 22 (USP22) could stabilise the expression of Sirtuin 1 (SIRT1)."
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"Lastly, ubiquitylation of USP22 mediated by the anaphase promoter complex/cyclosome (APC/C) induces USP22 protein degradation during the cell cycle [ xref ]."
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"Fourth, USP22 is ubiquitinated and degraded by CDC20-containing APC/C complex during cell exit from M phase, presumably to release the brake on CCNB1 degradation."
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"Besides, USP22 could remove poly-ubiquitin chain of CSN5, while CSN5 seemed no effect on USP22 ubiquitination (Fig. xref c, Fig. xref d)."
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"Conversely, treatment with the AKT-specific inhibitor facilitated USP22 protein degradation ( xref ), increased the USP22 ubiquitination ( xref ), and inhibited the AKT and USP22 interaction in breast cancer cells ( xref )."
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"Our data suggest that ATK-mediated phosphorylation of USP22 is critical for its stabilization because mutation of the phosphorylation residues increased USP22 ubiquitination and facilitated its proteasomal degradation."
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"Among these differentially ubiquitylated USP22 targets numerous DNA repair proteins, including XPC and RAD23B, were identified."
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