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USP8 deubiquitinates OGT. 8 / 8
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"A ubiquitination assay indicated that K117 was the key site on OGT deubiquitinated by USP8 (Figure 5J)."
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"Our results indicated that USP8 deubiquitinated OGT and affected the cystine uptake of HCC cells."
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"Second, USP8 decreased OGT polyubiquitination and promoted its protein stabilization in a DUB activity‐dependent manner."
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"Ectopic expression of USP8‐WT, but not USP8C , markedly decreased OGT ubiquitylation, indicating that the catalytical activity is essential for USP8 to regulate OGT protein levels."
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"Further analysis indicated that K117 is the key site on OGT deubiquitinated by USP8."
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"In this study, we unexpectedly find that USP8 could deubiquitylate and stabilize OGT in a deubiquitylation activity-dependent manner."
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"Conversely, ectopic expression of USP8‐WT, but not USP8‐C786A, markedly decreased OGT ubiquitylation in cells (Figure 5G)."
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"In vitro ubiquitylation assay indicated that USP8 directly decreased OGT ubiquitylation (Figure S4D, Supporting Information)."
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