IndraLab

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OTUB1 leads to the deubiquitination of RNF168. 4 / 4
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"Finally, the DUB OTUB1 inhibits RNF168 mediated ubiquitylation in a non catalytic fashion by binding to UBC13 and inhibiting the formation of Lys63 linked poly-ubiquitin chains [35 **]."
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"It has been reported that OTUB1 suppresses RNF168 dependent poly-ubiquitination by binding to and inhibiting UBC13, but independently of OTUB1 catalytic activity as a deubiquitinating enzyme (Nakada e[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Indeed, the ability of OTUB1 to inhibit RNF168 dependent ubiquitylation is independent of its catalytic activity, and is instead mediated by its binding to and inhibition of the E2 UBC13, which cooperates with RNF168, suggesting that E2 regulation could also represent a means to regulate the DDR pathway."
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"Remarkably, the ability of OTUB1 to inhibit RNF168 dependent ubiquitylation was independent of its catalytic activity, suggesting an unusual mechanism of action."
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