IndraLab

Statements

DROSHA binds USP36. 9 / 9
2 | 3 4
reach
"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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sparser
"Similarly, co-IP assays using lysates from cells transfected with V5-Drosha in the absence or presence of Flag-USP36 or its deletion mutants showed that Drosha also interacts with both the N-terminus and the C-terminus of USP36 ( xref and xref )."
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sparser
"Interestingly, the N-terminus of USP36 binds to Drosha stronger than the C-terminus (compare lane 6 with lane 4; xref )."
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"Knockdown of DGCR8 also did not reduce the interaction of USP36 with Drosha ( xref ; xref )."
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sparser
"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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biogrid
No evidence text available
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biogrid
No evidence text available
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reach
"Interestingly, the N-terminus of USP36 binds to Drosha stronger than the C-terminus (compare lane 6 with lane 4; Fig. 3C)."
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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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