IndraLab

Statements


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"Ultimately, we demonstrate that GSE1 is required for the recruitment of the deubiquitinase USP22 to the CoREST complex, potentially serving as a scaffold, and that loss of GSE1 inhibits deubiquitination of histone H2B at lysine 120, which was previously shown to facilitate γH2AX formation (11,35)."

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"Binding of USP22 to CoREST was independent of HDAC1 (Figure 6D) and also not affected by treatment with the HDAC inhibitor trichostatin A (TSA) (Supplementary Figure S6D)."

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"One of key requirements in this process seems to be the GSE1-dependent binding of USP22 to CoREST."

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"Of note, we observed that GSE1 is essential for the binding of USP22 to CoREST, suggesting a role as a scaffolder.Why has this multi-eraser complex gone unnoticed in previous research?"