IndraLab

Statements

OTULIN binds CTNNB1. 7 / 7
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"Interestingly, OTULIN-Y56D mutant overexpression induced more robust Wnt/β-catenin activation (Fig.  xref ), which may be a consequence of the increased interaction between β-catenin and OTULIN-Y56D mutant (Fig.  xref )."
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"In contrast, the interaction of OTULIN with β-catenin was substantially increased upon Dox treatment, which may be responsible for decreased linear ubiquitination and stabilization of β-catenin in cells exposed to genotoxic treatments (Supplementary Fig.  xref , Fig.  xref , lanes 1 and 2)."
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"Further characterization of domains required for the interaction between OTULIN and β-catenin revealed that the armadillo-repeats of β-catenin and the N-terminal region of OTULIN are required for their interaction (Fig.  xref and Supplementary Fig.  xref )."
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"However, while the Y56D mutation decreased OTULIN interaction with HOIP, it enhanced OTULIN association with β-catenin (Fig.  xref and Supplementary Fig.  xref ), suggesting that OTULIN Tyr56 phosphorylation may promote OTULIN interaction with β-catenin."
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"We speculate that the genotoxic stress-induced OTULIN phosphorylation at Tyr56 may not only increase the interaction between OTULIN and β-catenin but also enhance the LUBAC autoubiquitination and self-inhibition through dissociation from HOIP xref , which render OTULIN highly efficient in promoting β-catenin deubiquitination and stabilization upon DNA damage."
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"Inhibiting either c-Abl or DNA-PK with imatinib or Nu-7441 blocked Dox-enhanced OTULIN interaction with β-catenin while stabilizing OTULIN/HOIP interaction (Fig.  xref )."
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"We found genotoxic treatment enhanced the interaction between OTULIN and β-catenin."
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