IndraLab

Statements

USP35 binds SNAI1. 9 / 9
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"USP35 interacts with Snail1."
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"USP35 interacts with Snail1 to enhance its stability by removing its polyubiquitination chain."
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"We further explored the interaction between USP35 and Snail1 in GC cells using reciprocal IP."
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"As shown in Fig. 2F, deletion of the C-terminal USP domain abrogated the interaction with Snail1, indicating that the USP domain at the C-terminus of USP35 mediated the interaction between USP35 and Snail1."
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"To further examine the association between USP35 and Snail1 at the protein level, we measured the abundance of USP35 and Snail1 in various cancer cell lines, including liver, breast, prostate, and gastric cancers."
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"USP35 interacts with and deubiquitinates Snail1, thereby increasing Snail1 protein levels."
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"Further studies verified that USP35 can interact with Snail1 and that the USP catalytic domain at the C-terminus of USP35 participates in its interaction with Snail1."
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"Mechanistically, USP35 interacted with Snail1 and removed its polyubiquitinated chain, thereby increasing its stability."
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"As shown in Fig. xref F, deletion of the C-terminal USP domain abrogated the interaction with Snail1, indicating that the USP domain at the C-terminus of USP35 mediated the interaction between USP35 and Snail1."
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