IndraLab

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OTUD5 deubiquitinates GPX4. 12 / 12
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"OTUD5 mediates GPX4 deubiquitination to regulate its stability.Deletion of OTUD5 promotes ferroptosis and inhibits tumor growth.Wild type p53 inhibits OTUD5 transcription, thereby promoting GPX4 degradation and inhibiting the development of gastric cancer.OTUD5, GPX4 expression and p53 activity are highly correlated and correlates with clinical progression in STAD."
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"Co‐IP showed that OTUD5 interacts with GPX4 in cells (Figure 1E–H), which was further confirmed by their spatial proximity through immunofluorescence (Figure 1I).2.2 OTUD5 deubiquitinates and stabilises GPX4."
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"Therefore, identifying proteins that regulate GPX4 degradation is imperative for promoting ferroptosis without leading to the total elimination of GPX4.Next, we examined whether OTUD5 mediates the deubiquitination of GPX4 and found that overexpression of OTUD5 led to a significant reduction of GPX4 polyubiquitination (Figure 2J,K)."
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"Notably, the expression of wild‐type OTUD5 (OTUD5‐WT), but not the catalytically inactive mutant (OTUD5‐C224S) reduced GPX4 ubiquitination (Figure 2L)."
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"These data suggested that OTUD5 deubiquitinates GPX4, thereby enhancing its protein stability."
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"Additionally, we found that knockdown or depletion of OTUD5 markedly increased GPX4 ubiquitination (Figure 2N,O)."
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"In conclusion, these results demonstrated that OTUD5 mediates the K48‐linked deubiquitination of GPX4 and stabilises GPX4.2.3 OTUD5 suppresses ferroptosis via GPX4."
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"When experiencing I/R-induced AKI in mice or H/R-induced AKI in HK-2 cells, the deubiquitinase OTUD5 reportedly decreases the ubiquitination of GPX4, thus protecting GPX4 from TAX1BP1-dependent autophagy [131]."
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"Silencing OTUD5 increased GPX4 ubiquitination in HBMECs co-cultured with siTHBS1-AMφ-exo (Fig. 8G)."
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"OTUD5 increased GPX4 protein levels and decreased GPX4 ubiquitination in a dose‐dependent manner, whereas ectopic expression of OTUD5 did not affect GPX4 (Figure 4E,F; Figure S5E, Supporting Information), indicating that OTUD5 enzyme activity is indispensable for GPX4 protein stabilization."
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"Silencing OTUD5 increased GPX4 ubiquitination in HPMECs co-cultured with siGBP2-SMφ-EVs (Fig. 8H)."
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"Overexpression of OTUD5 blocked the detrimental effects of 4‐HNE on GPX4 ubiquitination and degradation in vivo and in vitro."
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