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USP36 sumoylates EXOSC10. 23 / 23
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"USP36 facilitates the SUMOylation of EXOSC10 by functioning as a SUMO E3 enzyme, thereby enhancing nucleolar RNA exoribonuclease functionality and cell proliferation."
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"Interestingly, USP36 markedly promoted EXOSC10 SUMOylation by both SUMO1 (Figure xref ) and SUMO2 ( xref )."
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"To test whether USP36 directly SUMOylates EXOSC10, we performed in vitro SUMOylation assays using recombinant proteins."
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"Notably, USP36 markedly increased EXOSC10 SUMOylation by SUMO1 in vitro , demonstrating that USP36 acts as a SUMO E3 for EXOSC10."
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"Furthermore, USP36 can also partake in the SUMOylation of EXOSC10 in conjunction with NPM1."
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"USP36 SUMOylates EXOSC10 in cells and in vitro."
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"Together, these data suggest that EXOSC10 SUMOylation by USP36 plays a critical role in rRNA processing."
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"These results suggest that USP36 acts as a SUMO ligase to SUMOylate EXOSC10 and promote the nucleolar RNA exosome function in ribosome biogenesis and cell growth."
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"Furthermore, USP36 could be detected in a protein complex together with EXOSC10 and NMP1 (Fig. 4B), suggesting that USP36 could be implicated in the SUMOylation of EXOSC10."
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"Inclusion of USP36 (1–420), but not USP36(421–800), caused detectable SUMOylation of wild-type EXOSC10, while the K583R mutant form of EXOSC10 could not be modified under the same conditions (Fig. 5C)."
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"USP36 SUMOylates EXOSC10 in cells and in vitro ."
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"Therefore, we examined whether USP36 promotes the SUMOylation of EXOSC10."
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"Together, these data suggest that EXOSC10 SUMOylation by USP36 plays a critical role in rRNA processing."
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"Moreover, Chen et al have shown that USP36 also mediates the SUMOylation of exosome component 10 (EXOSC10), critical for the RNA exosome function in ribosome biogenesis (Chen et al., 2023)."
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"Therefore, we examined whether USP36 promotes the SUMOylation of EXOSC10."
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"Interestingly, USP36 markedly promoted EXOSC10 SUMOylation by both SUMO1 (Figure 3B) and SUMO2 (Supplementary Figure S3C)."
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"Consistently, knockdown of USP36 significantly reduced the levels of EXOSC10 SUMOylation in cells by both exogenously expressed SUMO1 as determined by Ni -NTA PD assays (Figure 3C) and endogenous SUMO shown as the modified EXOSC10 band in IB assays (Figure 3D)."
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"USP36 promotes SUMOylation of EXOSC10 and hypoxia-induced disruption of their association inhibits the modification."
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"Notably, USP36 markedly increased EXOSC10 SUMOylation by SUMO1 in vitro, demonstrating that USP36 acts as a SUMO E3 for EXOSC10."
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"These data suggest that USP36-mediated EXOSC10 SUMOylation promotes the targeting of EXOSC10 to pre-rRNAs."
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"Therefore, it is also possible that EXOSC10 SUMOylation by USP36 could facilitate the assembly and stabilization of the exosome–TRAMP–adaptor protein complexes in the small subunit processome (SSU) and the large subunit processome (LSU)."
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"Consistently, the steady-state levels of EXOSC10 ubiquitination are below the level of detection (Supplementary Figure S3B), suggesting that under normal conditions, USP36 mainly acts to SUMOylate EXOSC10 to regulate its function, but not its levels, whereas its DUB activity may play a role in maintaining RNA exosome subunit proteins assembled in the RNA exosome in their deubiquitinated state in the nucleolus.Interestingly, we also found that USP36 associates with pre-rRNA (Figure 5C) and snoRNAs (not shown), indicating that USP36 itself could be an RNA-binding protein."
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"Therefore, it is also possible that EXOSC10 SUMOylation by USP36 could facilitate the assembly and stabilization of the exosome–TRAMP–adaptor protein complexes in the small subunit processome (SSU) and the large subunit processome (LSU)."
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