IndraLab

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USP20 increases the amount of SLC7A11. 4 / 4
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"Conversely, the deubiquitinating enzymes OTUB1 and ubiquitin specific peptidase 20 (USP20) mediate the deubiquitination of SLC7A11, thereby stabilizing SLC7A11 levels in cancer cells [6,122]."
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"We observed that USP20 depletion significantly reduced the protein expression of SLC7A11, and such effect could be blocked by the addition of MG132 (proteasome inhibitor) or overexpression of wild‐type USP20, but not its catalytically inactive mutant (Figures 4B and C)."
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"As expected, USP20 depletion remarkably reduced the protein levels of SLC7A11 without influence on the mRNA level (Figure 4A)."
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"Since USP20 is a DUB belonging to the ubiquitin‐specific processing protease family and USP20 depletion decreased SLC7A11 protein levels, suggesting that USP20 may control the protein stability of SLC7A11 via the Ub–proteasome system."
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