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USP22 deubiquitinates FOXM1. 5 / 5
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"Importantly, transient USP22 expression largely diminished FoxM1 ubiquitination (Fig. 3G)."
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"Our data indicate physical interaction between USP22 and FoxM1 is required for USP22-mediated suppression of FoxM1 ubiquitination, because mutation of cystines 61 and 63, which disrupts the zinc finger structure and its interaction with FoxM1 (Fig. 3I), totally abolished USP22 activity in suppressing FoxM1 ubiquitination (Fig. 3G)."
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"As expected, expression of the catalytically inactive USP22, through C185A mutation, failed to inhibit FoxM1 ubiquitination despite not altering its interaction with FoxM1 (Figures 3G and 3M)."
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"USP22 is required for human endometrial stromal cell proliferation and decidualization by deubiquitinating FoxM1."
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"Higher molecular weight bands were detected in FoxM1 immunoprecipitants, indicating FoxM1 is ubiquitinated possibly by its endogenous E3 ubiquitin ligases such as FBWX7.29 Importantly, transient USP22 expression largely diminished FoxM1 ubiquitination (Figure 3M)."
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