IndraLab

Statements

USP51 is phosphorylated. 9 / 9
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rlimsp
"The phosphorylation and activation of USP51 by CDK4/6 is necessary to deubiquitinate and stabilize ZEB1."
32296027
sparser
"Mechanistically, CDK4/6 deubiquitinates and stabilizes ZEB1 by activating and phosphorylating USP51."
37328395
sparser
"CDK4/6 kinases phosphorylate and stimulate deubiquitinase USP51, which stabilises ZEB1 [ xref ] (Fig. xref )."
37259089
sparser
"Moreover, we found a strong positive correlation between the expression of p -RB (an indicator of CDK4/6 activity), p -USP51 and ZEB1 in metastatic human breast cancer samples."
32195004
sparser
"Notably, the high expression of p -RB, p -USP51, and ZEB1 was significantly correlated with a poor clinical outcome."
32195004
sparser
"They found that CDK4/6 phosphorylate and activate the deubiquitinase USP51 , which is necessary for ZEB1 deubiquitination and stabilization."
39196911
sparser
"In terms of molecular mechanism, USP51 is phosphorylated and activated by CDK4/6, thus resulting in the deubiquitination and stabilization of ZEB1 protein."
35058607
sparser
"Over-expression of CDK6 causes the hyperphosphorylation of USP51 protein, causing its structural alteration and functional inactivation, and hence, USP51 protein cannot interact with ZEB1 protein [105[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
35878668
sparser
"In particular, it has been demonstrated that both these CDKs can bind and phosphorylate the deubiquitinase USP51 and DUB3, to control ZEB1 [ xref ] and SNAIL1 [ xref ] expression, respectively, thereby modulating the metastatic phenotype of cancer cells."
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