IndraLab

Statements

SNAI1 binds USP36. 17 / 19
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"Stable protein complexes between USP36 and Snail1 were readily detected in the nucleoli even in the presence of 500 mM NaCl (Fig.  xref )."
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"Lys157 of Snail1 is essential for Snail1-USP36 complex formation and ribotoxic stress-induced Snail1 nucleolar accumulation."
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"To address whether USP36 binds to ubiquitinated Snail1, we employed a specific E1 inhibitor, TAK-243, to block protein ubiquitination."
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"As shown in Supplementary Fig.  xref , USP36 effectively interacted with Snail1 regardless of the status of its ubiquitination."
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"To identify binding segments important for USP36-Snail1 interaction, we constructed a series of truncation mutants."
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"As shown in Fig.  xref , the N-terminus of USP36 (1–423 aa) interacted with the C-terminus of Snail1 (152–264 aa)."
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"Indeed, further experiments showed that the C2H2-type 1 Zinc finger (154–176 aa, ZnF1) of Snail1 protein is responsible for USP36-Snail1 interaction (Fig.  xref )."
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"By contrast, ectopic expression of ATXN3 upregulated both Snai11 WT and Snail1 K157R (Fig.  xref ), suggesting that K157 is critical for Snail1-USP36 interaction."
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"Notably, while Snai11 WT and Snail1 K157R exhibited a similar half-life in the absence of ribotoxic stress, HHT significantly prolonged the protein half-life of Snai11 WT , but not Snail1 K157R (Fig.  xref ), indicating that USP36–Snail1 interaction is critically important in the stabilization of Snail1 in the nucleoli upon ribotoxic stress."
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"Next, we investigated whether USP36-Snail1 interaction is required for Snail1 nucleolar accumulation."
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"Together, these results indicate that K157 of Snail1 is essential for Snail1-USP36 protein complex formation and Snail1 nucleolar accumulation upon ribotoxic stress."
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"Activation of nucleolar USP36-Snail1 axis promotes ribosome biogenesis to promote cancer cell survival in response to ribotoxic stress."
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"We next investigated the biological significance of the nucleolar USP36-Snail1 axis."
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"Our abovementioned data indicate that activation of the nucleolar USP36-Snail1 axis promotes ribosome biogenesis to sustain cancer cell survival in response to ribotoxic stress, exemplified by HHT."
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"We demonstrate that while Lys157 of Snail1 is critical for USP36-Snail1 protein complex formation, Lys146 and Lys206 on Snail1 are two key amino acid residues deubiquitinated by USP36."
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"Lys157 of Snail1 is essential for Snail1-USP36 complex formation and ribotoxic stress-induced Snail1 nucleolar accumulation."
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"Since the USP36 protein bears several NoLS , it is plausible that USP36 binds to and shuttles Snail1 into the nucleolus and stabilizes Snail1."
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