IndraLab

Statements

ZMYND8 binds OTUD4. 8 / 8
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"Consistent with this hypothesis, endogenous co-immunoprecipitation (Co-IP) assays in MDA-MB-231 and 4T1 cells confirmed the interaction between ZMYND8 and OTUD4 ( xref D)."
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"Co-IP experiments demonstrated that endogenous ZMYND8 interacts with OTUD4, suggesting that OTUD4 may regulate ZMYND8 protein stability."
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"The results indicated an interaction between ZMYND8 and the deubiquitinase OTUD4 ( xref A)."
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"RosettaDock analysis predicted a direct interaction between ZMYND8 and OTUD4 ( xref B)."
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"Our mechanistic investigations reveal that OTUD4 directly interacts with ZMYND8 and catalyzes its deubiquitination at evolutionarily conserved residues (K294 in human, K318 in murine) within the PWWP domain."
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"Co-immunoprecipitation assays showed that both OTUD4 catalytic mutants retained the ability to physically associate with ZMYND8 at levels comparable to wild-type OTUD4 ( xref C), indicating that loss of catalytic activity does not impair OTUD4–ZMYND8 binding."
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"Furthermore, in situ proximity ligation assay (PLA) validated the direct in situ interaction between ZMYND8 and OTUD4 ( xref E)."
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"Inhibitors designed to disrupt the OTUD4–ZMYND8 interaction or impede DDX3X–CK1ε complex formation may attenuate WNT pathway activation and reverse local immunosuppression."
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