IndraLab

Statements

USP37 binds Snail1. 12 / 12
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"USP37 interacts with and deubiquitinates Snail1 directly."
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"We further investigated the interaction between USP37 and Snail1."
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"Given that the SRD domain is essential for the interaction between USP37 and Snail1, we evaluated its effect on Snail1 ubiquitination in HEK293T cells."
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"Therefore, the SRD domain is also crucial for USP37 mediated Snail1 deubiquitination and the interaction between USP37 and Snail1."
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"Overall, these results demonstrate that USP37 interacts with and deubiquitinates Snail1 directly."
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"To explore whether the interaction between Snail1 and USP37 requires Snail1 phosphorylation, we utilized CIP to remove phosphate groups from the substrate proteins."
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"Strikingly, Co-IP experiments showed that the interaction between USP37 and Snail1 was strongly impeded by CIP intervention."
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"Since GSK-3beta is the major kinase involved in Snail1 phosphorylation in the SRD region, the GSK-3beta inhibitor LiCl was used to assess GSK-3beta inhibition in the interaction of USP37 and Snail1."
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"As shown in Figure XREF_FIG B, LiCl treatment also significantly disrupted the USP37 and Snail1 interaction."
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"Co-IP results showed that GSK-3beta siRNAs diminished approximately 60% of the interaction of USP37 and Snail1."
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"We also determined that USP37 interacts with and deubiquitinates Snail1 directly, which is transcriptionally activated by PLAGL2."
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"However, in cells with high expression of USP37, phosphorylated Snail1 promotes the mutual binding of USP37 and Snail1, and the ability of USP37 to bind to phosphorylated Snail1 is significantly enhanced."
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