IndraLab

Statements

OTUB1 leads to the deubiquitination of RNF168. 6 / 6
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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."
21056014
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"Otub1 was shown to suppress RNF168-dependent ubiquitination in a non-catalytic manner, by interacting with and inhibiting Ubc13 ( Nakada et al., 2010 )."
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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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"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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"Rather, ataxin-3 was acting similarly to another unconventional DUB, OTUB1, that suppresses RNF168-mediated polyubiquitination by interacting with and inhibiting the Ubc13 E2-Ub-conjugating enzyme (Nakada et al. 2010)."
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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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