IndraLab

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DGCR8 binds USP36. 6 / 10
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"To examine where USP36 binds to Drosha and DGCR8, we also performed co-IP and IB experiments using a panel of Flag-DGCR8 mutants (Fig. 3E and F) and Flag-Drosha mutants (Fig. 3G and H)."
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"It is likely that SUMOylation of DGCR8 may induce confirmational changes that favor the microprocessor complex targeting of pri-miRNAs and thus increase the activity of Drosha-mediated processing of the pri-miRNAs.Our binding domain mapping results reveal that USP36 binds to DGCR8 and Drosha via distinct domains, suggesting that the three proteins form a multiprotein complex."
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"As shown in xref , knockdown of Drosha did not abolish the interaction of USP36 with 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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"As show in xref , USP36 interacts with the C-terminus region of DGCR8 that contains two dsRBD domains."
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"Both DGCR8 and Drosha can bind to the N-terminus and C-terminus of USP36 albeit DGCR8 binds strongly to the C-terminus of USP36 whereas Drosha binds strongly to the N-terminus of USP36."
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