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USP5 deubiquitinates CTNNB1. 15 / 15
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"Ubiquitin-specific peptidase 5 facilitates cancer stem cell-like properties in lung cancer by deubiquitinating beta-catenin."
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"USP5 promotes stemness properties by deubiquitinating beta-catenin."
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"Ma et al. [ 38 ] found that USP5 could activate the Wnt/β-catenin pathway by deubiquitinating and stabilizing β-catenin protein in non-small cell lung cancer, which results in promotion of cell prolif[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Collectively, these data suggest that USP5 deubiquitinates β-catenin, promotes β-catenin stability, and subsequently promotes Wnt signaling pathway activity in lung cancer cells.To confirm the role of β-catenin in USP5-mediated stemness, we silenced the β-catenin expression in USP5-overexpressing A549 cells and determined the sphere-forming ability (Additional file 1: Figure S5D)."
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"Inhibition of USP5 by small molecules enhances beta-catenin ubiquitination and suppresses stemness properties and cell motility."
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"Mechanistically, Wnt signaling signatures were identified to be clinically related to USP5 expression, and our data showed that USP5 physically interacted with β-catenin to cause β-catenin deubiquitination and stabilization, thereby stimulating Wnt signaling."
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"Here, our findings provide new insights indicating that USP5 interacts with β-catenin, causes β-catenin deubiquitination, prolongs the β-catenin protein half-life, and thus increases the expression of Wnt/β-catenin downstream target genes in lung cancer.Our study showed WP1130 inhibited cell motility and cancer stemness in lung cancer."
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"Mechanistically, we found that USP5 deubiquitinated beta-catenin, prevented ubiquitination mediated beta-catenin degradation and promoted beta-catenin nuclear accumulation, leading to the activation of Wnt and beta-catenin signal pathway in NSCLC cells."
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"DEPDC1B-mediated USP5 deubiquitination of beta-catenin promotes breast cancer metastasis by activating the wnt/beta-catenin pathway."
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"Furthermore, we also revealed a novel mechanism in DEPDC1B-mediated USP5 deubiquitination of β-catenin, which led to the activation of the wnt/β-catenin signaling pathway and ultimately promoted breast cancer cell metastasis."
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"In non-small-cell lung cancer and trophoblast cells, USP5 can deubiquitinate and stabilize β-catenin and activate the wnt/β-catenin signaling pathway (43–45)."
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"Mechanistically, we found that <span class="match term0">USP5</span> deubiquitinated <span class="match term1">BETA-CATENIN</span>, prevented ubiquitination mediated <span class="match term1">BETA-CATENIN</span> degradation and promoted <span class="match term1">BETA-CATENIN</span> nuclear accumulation, leading to the activation of Wnt/<span class="match term1">BETA-CATENIN</span> signal pathway in NSCLC cells"
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"First, mechanistically, how DEPDC1B, USP5, and β-catenin interact, the location of the binding sites, how DEPDC1B mediates the deubiquitination of β-catenin by USP5, and whether DEPDC1B has enzyme activity remain to be further explored."
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"As previously described, USP5 can deubiquitinate and stabilize β-catenin, leading to β-catenin nuclear accumulation and activation ( Fig. 3 b) [ 38 ]."
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"Finally, we found that in breast cancer cells DEPDC1B mediates the deubiquitination of β-catenin by USP5, stabilizes the β-catenin protein level, promotes nuclear translocation, activates the wnt/β-catenin signaling pathway, and ultimately promotes the transfer of breast cancer cells (Fig. 8)."
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