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USP36 binds EXOSC10. 18 / 23
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"As shown in Figure xref , knockdown of EXOSC10 abrogated the interaction of USP36 with the exosome core components EXOSC3 and EXOSC4, suggesting that USP36 interaction with EXOSC10 is critical for its interaction with the core RNA exosome complex."
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"We found that RNase treatment indeed reduced, but did not abolish, the interaction between USP36 and EXOSC10 in both 293 (Figure xref ) and HeLa cells ( xref ), whereas the interaction of USP36 with RPL30 and RPS27a was abolished by the RNase treatment, suggesting that USP36 may directly interact with EXOSC10 and that this interaction is facilitated by RNA-containing pre-ribosome particles."
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"As shown in Figure xref , recombinant His-USP36 protein purified from bacteria ( xref ) was specifically bound by purified GST–EXOSC10, but not GST alone, indicating that USP36 directly interacts with EXOSC10 in vitro ."
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"EXOSC10 and USP36 interact via their C-terminal domains."
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"To understand how USP36 interacts with EXOSC10, we mapped the binding domains between USP36 and EXOSC10 using co-IP–IB assays."
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"As shown in Figure xref , the C-terminal nucleolar localization signal (NoLS)- ( xref , xref ) containing region (amino acids 801–1121), but not the N-terminal USP domain-containing (amino acids 1–420) and the middle (amino acids 421–800) regions, interacts with EXOSC10, indicating that EXOSC10 binds to the C-terminus of USP36 (Figure xref )."
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"Furthermore, RNase treatment also reduced, but did not abolish, the interaction of USP36 with the C-terminal Lasso domain of EXOSC10 ( xref ) or the interaction of EXOSC10 with USP36 801–1121 ( xref )."
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"Together, these results indicate that the C-terminal region of USP36 directly interacts with the C-terminal Lasso domain of EXOSC10 (Figure xref , xref ) that can also be facilitated by the association with RNA."
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"We performed co-IP assay using the lysates from the isolated nucleolar fraction and further confirmed that USP36 interacts with EXOSC10 in the nucleolus (Figure xref )."
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"Although expression level of USP36 was not affected significantly by hypoxia (Fig. 4C), hypoxic treatment abolished the interaction between USP36 and EXOSC10 without significantly affecting the interaction between NPM1 and EXOSC10 (Fig. 4B)."
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"However, this interaction between USP36 and EXOSC10 is disrupted under hypoxic conditions, leading to the loss of SUMOylation of EXOSC10 [ xref ]."
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"While USP36 directly interacts with EXOSC10, it does not markedly influence the levels of EXOSC10 or other examined exoribonuclease subunits."
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"Also, the K583R mutation does not affect the interaction of EXOSC10 with USP36 ( xref )."
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"However, this interaction between USP36 and EXOSC10 is disrupted under hypoxic conditions, leading to the loss of SUMOylation of EXOSC10 [20]."
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"Although expression level of USP36 was not affected significantly by hypoxia (Fig. xref C), hypoxic treatment abolished the interaction between USP36 and EXOSC10 without significantly affecting the interaction between NPM1 and EXOSC10 (Fig. xref B)."
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"Co-IP assays confirmed that Flag-USP36 binds to EXOSC10, the ‘cap’ subunit EXOSC3/hRrp40 and the ‘ring’ subunit EXOSC4/hRrp41 in 293 (Figure 1C) and HeLa (Supplementary Figure S1D) cells, but not with Dis3 (Figure 1D), the catalytical subunit of the RNA exosome in the nucleoplasm, consistent with the notion that USP36 interacts with the nucleolar RNA exosome."
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"As shown in Figure 1G, knockdown of EXOSC10 abrogated the interaction of USP36 with the exosome core components EXOSC3 and EXOSC4, suggesting that USP36 interaction with EXOSC10 is critical for its interaction with the core RNA exosome complex."
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"We found that RNase treatment indeed reduced, but did not abolish, the interaction between USP36 and EXOSC10 in both 293 (Figure 1H) and HeLa cells (Supplementary Figure S1G), whereas the interaction of USP36 with RPL30 and RPS27a was abolished by the RNase treatment, suggesting that USP36 may directly interact with EXOSC10 and that this interaction is facilitated by RNA-containing pre-ribosome particles."
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