IndraLab

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OTUB1 activates SLC7A11. 5 / 5
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"Consistent with the role of a DUB in regulating protein stability, OTUB1 overexpression resulted in reduced SLC7A11 ubiquitination and increased SLC7A11 protein half-life and steady protein levels; conversely, OTUB1 deletion in a variety of cancer cell lines resulted in a significant decrease in SLC7A11 protein levels."
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"Taken together, although the precise mechanism by which OTUB1 induces SLC7A11 stabilization requires further elucidation, it is very likely that the binding between OTUB1 and SLC7A11 as well as OTUB1 's ability of inhibiting E2 conjugating enzymes recruited by the unknown E3 ligase contribute to SLC7A11 stabilization induced by OTUB1."
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"Evidence suggests that the deubiquitinase OTUB1, usually overexpressed in cancers, replicates the ferroptosis process and promotes tumor development by stabilizing the cystine transporter SLC7A11 (Gan, 2019)."
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"For example, in a non neuronal setting, induction of ferroptosis with the small molecule erastin is suppressed by the ubiquitin ligase NEDD4 [XREF_BIBR], whilst the DUBs OTUB1 and USP7 promote ferroptosis by stabilising the mediators SLC7A11 and p53, respectively [XREF_BIBR, XREF_BIBR]."
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"As shown in XREF_FIG, the stability of SLC7A11 was effectively rescued by OTUB1 (C91A) but not by OTUB1 (D88A), suggesting that OTUB1 promotes SLC7A11 stabilization independent of its deubiquitinase activity."
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