IndraLab

Statements

E3_Ub_ligase inhibits USP22. 6 / 6
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"Therefore, APC and CDC20 E3 ligase complex promotes USP22 protein degradation, presumably allowing CCNB1 degradation for cells to exit M phase."
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"USP22 is degraded by the APC/C E3 ubiquitin ligase complex, which also targets CCNB1 for destruction [XREF_BIBR, XREF_BIBR], thereby allowing cells to exit from mitosis, presumably by facilitating CCNB1 degradation."
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"In contrast, the APC and CDC20 E3 ligase complex negatively regulates USP22 activity by targeting it for degradation, presumably allowing CCNB1 downregulation so that cells can exit mitosis and enter anaphase."
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"To identify the E3 ligase that degrades USP22, we tested the interaction between USP22 and FBW7, CDC20, and CDH1, all of which are active during exit from mitosis [XREF_BIBR, XREF_BIBR]."
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"Moreover , anaphase-promoting complex cell division cycle protein 20 ( APCCDC20 ) , an E3 ubiquitin ligase , promotes USP22 degradation in a cell cycle-dependent manner ( 61 ) ."
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"Our study demonstrates that USP22 is also a substrate of the APC/C E3 ligase complex, which degrades USP22 during cell exit from M phase."
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