IndraLab

Statements

USP24 binds BRD. 7 / 7
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"In this study, we found that the deubiquitinase USP24 interacted with BRD through its C-terminus increased the levels of most BRD-containing proteins through increasing their protein stability by the removal of ubiquitin from Lys391/Lys400 of the BRD."
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"Loss of the interaction motif of USP24 eliminated the ability of USP24 to stabilize BRD-containing proteins and abolished the effect of USP24 on cancer progression, including its inhibition of cancer cell proliferation and promotion of cancer cell migration, suggesting that the interaction between USP24 and the BRD is important for USP24-mediated effects on cancer progression."
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"Because USP24 could interact with more than one BRD-containing protein, we hypothesized that USP24 can interact with the BRD, which is common to all BRD-containing proteins."
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"2153) was sufficient for the interaction between USP24 and BRD (Fig.  xref B)."
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"Owing to the absence of structural information on the interaction between USP24 and the BRD, we generated a structural model of the catalytic domain of human USP24 (USP24-CD) by using the SWISS-MODEL server, and a complex structural model of the interaction between USP24-CD and the second BRD of human BRD2 (BRD2-BD2) was built up by using the ZDOCK server, which provided a structural view to understand the interactions between USP24-CD and BRD2-BD2 (Fig.  xref G(a))."
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"Finally, we also used a structural model of USP24 built based on USP7 as a parent template to study the structural interaction between USP24 and the BRD (Fig.  xref G)."
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"BRD interacts with the C-terminus of USP24."
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