IndraLab

Statements

USP38 binds ADAR. 10 / 10
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"Subsequently, we used the online web tool DMFold () to predict the structure of the USP38 and ADAR complex."
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"DMFold predicted five structures for the USP38–ADAR complex."
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"These findings demonstrate that the interaction between USP38 and ADAR is mediated through their C-terminal enzymatic catalytic regions."
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"Structural predictions suggest that ADAR and USP38 interact within their enzymatic activity domains, raising the question of whether ADAR induces conformational changes in USP38 to modulate its enzymatic activity."
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"More importantly, our results provide a rationale for targeting the ADAR–USP38 axis for the treatment of ESCC."
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"To further confirm the interaction between USP38 and ADAR, we coexpressed USP38 and ADAR proteins tagged with different tags in HEK293T cells and then analyzed the interaction between USP38 and ADAR through IP."
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"Endogenous coimmunoprecipitation results also showed that stable protein complexes between ADAR and USP38 were readily detected ( xref , B and C )."
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"These results indicate that USP38 and ADAR interact in the cell nucleus."
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"The interaction between USP38 and ADAR depends on its enzymatic active region."
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"To clarify the structural domains involved in the USP38 and ADAR interaction, a series of deletion mutants of USP38 (WT (1-1042AA), N-term (1-400AA), C-term (401-1042AA)) and ADAR (WT (1-931AA), ΔZD (deletion of 1-71AA), ΔRBD (deletion of 207-499AA), and ΔDD (deletion of 591-926AA)) were used for IP analyses."
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