IndraLab

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OTUD7B binds KDM1A. 15 / 15
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"These data highlight a dose‐limiting transcriptional regulation of genes involved in cell proliferation by OTUD7B–LSD1 axis, which might explain why this pathway confers a proliferative advantage in a context‐dependent manner."
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"Using recombinant proteins, we concluded that OTUD7B can directly interact with LSD1 in vitro (Figure xref , Supporting Information)."
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"Taken all together, these results suggest that OTUD7B binds and stabilizes LSD1 via abrogating its ubiquitination‐dependent proteasomal degradation."
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"Therefore, perturbation of OTUD7B–LSD1 axis results in changes in both activating and repressive chromatin modification marks, providing a plausible mechanism for altered gene transcription due to OTUD7B loss."
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"We next explored the clinical implications of OTUD7B–LSD1 signaling."
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"Using OLco‐regulated gene sets revealed that loss of OTUD7B or LSD1 resulted in a significantly reduced expression of metastatic genes (Figure xref , Supporting Information), providing potential mechanistic clues explaining suppressed metastatic ability due to impaired OTUD7B–LSD1 signaling."
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"2.1 OTUD7B Binds LSD1 and Regulates Its Stability."
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"OTUD7B Binds LSD1 and Regulates Its Stability."
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"In addition to USP22 and USP28, ectopic OTUD7B also bound robustly to endogenous LSD1 (Figure  1A )."
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"In addition to USP22 and USP28, ectopic OTUD7B also bound robustly to endogenous LSD1 ( Figure   xref )."
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"Of note, both wild type (WT) and the catalytically inactive form (CI, C194A/H358R) of OTUD7B bound ectopic LSD1 (Figure S1C,D, Supporting Information)."
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"Interestingly, when compared to LSD1–CoREST complex, endogenous OTUD7B–LSD1 complex is readily detectable but with much less abundance, indicating OTUD7B may interact with LSD1 in a transient manner (Figure 1B)."
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"Interestingly, when compared to LSD1–CoREST complex, endogenous OTUD7B–LSD1 complex is readily detectable but with much less abundance, indicating OTUD7B may interact with LSD1 in a transient manner (Figure  xref )."
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"Taken all together, these results suggest that OTUD7B binds and stabilizes LSD1 via abrogating its ubiquitination‐dependent proteasomal degradation.2.2 OTUD7B Is a Bona Fide LSD1 Deubiquitinase."
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