IndraLab

Statements

OTUD3 binds YY1. 11 / 11
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"Importantly, interactions between endogenous YY1 and OTUD3 were observed in SW480, LoVo and DLD1 cells (Fig. xref and Supplementary Fig. xref )."
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"OTUD3 directly binds to and deubiquitinates YY1, preventing its proteasomal degradation."
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"Notably, the OTUD3-YY1 axis provides a compelling link between inflammatory signals and CRC progression, consistent with YY1 upregulation in inflammation-associated cancers [ xref ]."
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"Furthermore, PLK1 mediates OTUD3 S326 phosphorylation, which further enhances OTUD3 binding and deubiquitination of YY1."
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"Importantly, interactions between endogenous YY1 and OTUD3 were observed in SW480, LoVo and DLD1 cells (Fig. 1C and Supplementary Fig. S1B)."
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"Furthermore, in vitro pull-down assays with purified recombinant proteins showed that YY1 directly bound GST-OTUD3, not GST control (Fig. 1D)."
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"An in-situ proximity ligation assay (PLA) was performed to identify the interactions between endogenous YY1 and OTUD3 in CRC cells."
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"Then, the immunoprecipitation assays confirmed that up-regulated PLK1 promoted the physical binding between OTUD3 and YY1, but failed to promote the binding between OTUD3 mutation (S326A) and YY1 (Fig. 5L–N and Supplementary Fig. S5A, B)."
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"We found that OTUD3 directly interacts with YY1."
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"OTUD3 interacts with YY1."
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"Treatment with the PLK1 inhibitor, HMN-214, significantly inhibited the binding between OTUD3 and YY1 (Supplementary Fig. S5C, D)."
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