IndraLab

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USP36 sumoylates DGCR8. 20 / 20
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"USP36 interacts with the DGCR8-Drosha complex and promotes DGCR8 SUMOylation specifically by SUMO2."
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"USP36 interacts with the microprocessor complex and promotes DGCR8 SUMOylation, specifically modified by SUMO2."
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"USP36 SUMOylates DGCR8."
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"Intriguingly, coexpression of USP36 markedly increased the SUMOylation of DGCR8 modified by SUMO2, but not SUMO1."
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"The Ubiquitin-specific Protease USP36 Associates with the Microprocessor Complex and Regulates miRNA Biogenesis by SUMOylating DGCR8."
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"USP36 interacts with the microprocessor complex and promotes DGCR8 SUMOylation, specifically modified by SUMO2."
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"Significance:. This study identifies that USP36 mediates DGCR8 SUMOylation by SUMO2 and is critical for miRNA biogenesis."
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"Similarly, DGCR8 SUMOylation by USP36 does not affect the DGCR8-Drosha microprocessor complex formation but promotes DGCR8 binding to pri-miRNAs, suggesting that SUMOylation of DGCR8 by USP36 increases its affinity to pri-miRNAs."
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"For instance, the ubiquitin-specific protease (USP36) has been found to associate with the Microprocessor complex and regulate miRNA biogenesis by SUMOylating DGCR8 [21]."
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"Of note, we observed that USP36 specifically promotes DGCR8 SUMOylation by SUMO2, but not SUMO1, although it can promote protein SUMOylate by either SUMO1 or SUMO2 ( xref )."
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"USP36 SUMOylates DGCR8."
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"This interaction occurs between USP36 and the microprocessor complex, promoting the SUMOylation of DGCR8, with a particular emphasis on SUMO2-modified DGCR8."
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"USP36 interacts with the DGCR8-Drosha complex and promotes DGCR8 SUMOylation specifically by SUMO2."
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"Therefore, our results suggest that SUMOylation of DGCR8 by USP36 promotes DGCR8 association with pri-miRNA and thus the pri-miRNA processing."
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"To understand the biological function of DGCR8 SUMOylation by USP36, we established the tet-inducible expression of WT DGCR8 and the SUMOylation-defective DGCR8 3KR mutant in HeLa cells ( xref ) and perform cell proliferation assays."
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"The effect of USP36 in promoting DGCR8 SUMOylation does not depend on its DUB activity, as the DUB catalytically inactive but SUMO ligase active mutant as we have described previously (27), H382A (the DUB catalytic protein acceptor His 382 is mutated to Ala), promoted DGCR8 SUMOylation as efficiently as WT USP36 (Supplementary Fig. S4C)."
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"Therefore, our results suggest that SUMOylation of DGCR8 by USP36 promotes DGCR8 association with pri-miRNA and thus the pri-miRNA processing."
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"In this study, we report that USP36 regulates miRNA biogenesis by SUMOylating DGCR8."
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"Similarly, DGCR8 SUMOylation by USP36 does not affect the DGCR8-Drosha microprocessor complex formation but promotes DGCR8 binding to pri-miRNAs, suggesting that SUMOylation of DGCR8 by USP36 increases its affinity to pri-miRNAs."
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"It is likely that pri-miRNAs may associate with the microprocessor complex in the nucleoplasm and then translocated into the nucleolus, possibly by binding an anchor protein nucleolin as suggested (34, 39) and USP36 may stabilize the complex and facilitate the miRNA processing activity via SUMOylating DGCR8 in the nucleolus.Of note, we observed that USP36 specifically promotes DGCR8 SUMOylation by SUMO2, but not SUMO1, although it can promote protein SUMOylate by either SUMO1 or SUMO2 (27)."
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