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USP51 binds DGCR8. 5 / 5
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"Moreover, the interaction between DGCR8 and USP51 was enhanced in a time-dependent manner after irradiation of LM2 cells (Supplementary Fig.  xref ), and this increased interaction was observed with endogenous proteins (Fig.  xref )."
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"To validate the direct interaction between USP51 and DGCR8, we expressed and purified SFB-USP51 and MBP-DGCR8 proteins, and in vitro pulldown assays demonstrated that USP51 bound to DGCR8 (Fig.  xref ), indicating that DGCR8 may be directly regulated by USP51."
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"Furthermore, our results demonstrate that USP51 directly binds and deubiquitinates DGCR8 in a K48 linkage-specific manner, and that this deubiquitination is enhanced by IR treatment."
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"Collectively, these results suggest that after irradiation, ATM-dependent phosphorylation of DGCR8 at S677 is crucial for the recruitment of the DGCR8-RNF168 complex to MDC1 and RNF8 at DSBs, as well as the subsequent interaction of DGCR8 with USP51, DGCR8 deubiquitination, histone ubiquitination, and DSB repair."
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"Consistent with the results in Supplementary Fig.  xref , the interaction between WT DGCR8 and USP51 was enhanced at 8 h, but not at 1 h, after IR, and this increased interaction was abolished by the phosphodeficient mutation (S677A), but not by the phosphomimetic mutation (S677D) (Fig.  xref )."
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