IndraLab

Statements

USP51 activates ZEB1. 10 / 10
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"Conversely, overexpression of USP51 in epithelial cells resulted in upregulation of ZEB1 and mesenchymal markers."
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"Among DUBs, ubiquitin specific peptidase 51 (USP51) binds to the N-terminal of ZEB1 and increases ZEB1 protein stability in breast cancer cell lines [XREF_BIBR]."
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"In vitro , ectopic expression of USP51 up-regulates Zeb1 and the mesenchymal markers N-cadherin and Vimentin [ 77 ]."
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"Unsupervised heatmap clustering revealed cluster 12 and 14 to have close homology in terms of the high expression of USP51 and CASP8AP2 which are both known to promote ZEB1 protein stabilization [30, 31] (Supplementary Fig. 3B)."
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"USP51 depletion inhibited the invasion of mesenchymal-like breast cancer cells by downregulating ZEB1 protein and mesenchymal marker expression and promoting E-cadherin upregulation."
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"On the other hand, overexpression of USP51 led to the upregulation of ZEB1 and mesenchymal markers in epithelial cells [13]."
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"Thus , the deubiquitinases ( DUBs ) were involved in counteracting polyubiquitination and proteasomal degradation of ZEB1 [ 40 ] ; these DUBs include USP51 , which upregulated ZEB1 and the mesenchymal markers by binding , deubiquitinating , and stabilizing ZEB1 [ 41 ] ."
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"Moreover, we showed that USP51 promotes tumor metastasis and invasion through regulating ZEB1, which is a key transcriptional factor that induces the malignant progression of lung adenocarcinoma."
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"ZEB1 has illustrated to be modulated by USP7, USP22 and USP51 in cancers."
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"Intriguingly, the loss of USP51 deubiquitinase decreases the half-life of endogenous ZEB1 protein, whereas MG132 induces the polyubiquitination of ZEB1 in LM2 cells (a lung metastatic subline of MDA-MB-231 cells) [91]."
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