IndraLab

Statements

USP22 is phosphorylated. 23 / 34
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"Our data suggest that ATK-mediated phosphorylation of USP22 is critical for its stabilization because mutation of the phosphorylation residues increased USP22 ubiquitination and facilitated its proteasomal degradation."
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"Moreover, cyclin B1-Cdk1 leads to USP22 phosphorylation on residues Thr147 and Ser237, which in turns promotes its deubiquitinase activity."
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"Notably, USP22 phosphorylation levels are positively associated with EPI and with downstream pathways involving both FOXO1 and ATGL in breast cancers."
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"Only weak USP22 phosphorylation was detected in HCT116 cells, presumably catalyzed by endogenous CDK1, and CDK1 overexpression significantly increased USP22 phosphorylation."
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"In addition, expression of the constitutively active form of CDK1 (CDK1/AF) [ xref , xref ] further enhanced USP22 phosphorylation in HCT116 cells ( xref )."
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"Moreover, mutation of the aspartic acid at position 146 of CDK1 (CDK1/D146N), which is a kinase-inactive mutant [ xref ], completely abolished its ability to promote USP22 phosphorylation ( xref )."
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"In an in vitro kinase assay, co-incubation of the purified GST-USP22 fusion proteins and the constitutive forms of CDK1 (CDK1/AF) immunoprecipitated from transiently transfected HCT116 cells confirmed USP22 phosphorylation by CDK1 ( xref )."
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"Endogenous USP22 was phosphorylated in G2/M phase, but not in G1 phase, as the phosphorylated forms of USP22 were detected in cells treated with thymidine-nocodazole but not double thymidine ( xref )."
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"These findings show that CDK1 is a kinase that catalyzes USP22 phosphorylation in a cell cycle-specific manner."
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"These results indicate that T147 and S237 are the potential CDK1 phosphorylation sites and imply that these residues have important functions in CDK1-mediated USP22 phosphorylation."
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"Replacing both T147 and S237 with alanine (AA) completely abolished USP22 phosphorylation and led to decreased CCNB1 protein levels even when CDK1 was co-expressed in HCT116 cells ( xref and xref )."
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"To study the cell cycle-specific functions of CDK1-mediated USP22 phosphorylation, in addition to the phosphorylation-defective USP22/AA mutant, we generated a phosphorylation-mimetic mutant by replacing both T147 and S237 with aspartic acid (D) (USP22/DD)."
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"In contrast, the degradation of CCNB1 was blocked in HCT116-USP22/DD cells, suggesting that CDK1-mediated USP22 phosphorylation enhances its ability to stabilize CCNB1 ( xref ) and may be involved in mitotic progression ( xref )."
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"To test our hypothesis, we purified USP22 protein from HCT116 cells, treated the protein with calf intestinal alkaline phosphatase, which presumably suppresses USP22 phosphorylation, and then co-incubated it with ubiquitinated CCNB1 protein."
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"Therefore, USP22 phosphorylation is correlated with its cell cycle-specific deubiquitinase activity."
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"Further treatment with the AKT-specific inhibitor largely diminished EPI-induced USP22 phosphorylation ( xref ), indicating that AKT is a kinase for USP22 phosphorylation in breast cancer cells upon EPI stimulation."
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"Interestingly, USP22 activity is regulated by CDK1, which catalyzes USP22 phosphorylation to elevate USP22 ability in CCNB1 deubiquitination and stabilization."
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"These results indicate that EPI stabilizes USP22 through AKT-mediated USP22 phosphorylation."
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"We then generated a USP22 mutant by replacing all five identified S/T residues with alanine (A) (USP22-TP) and confirmed that the mutation totally abolished AKT-mediated USP22 phosphorylation ( xref )."
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"Consistent with our in vitro findings ( xref ), EPI treatment augmented USP22 phosphorylation and protein expression in the tumor tissues (fig."
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"These results indicate that EPI induces USP22 phosphorylation both in vitro and in tumor tissues in an AKT-dependent manner."
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"We then analyzed the phospho-USP22 (p-USP22) levels by IHC staining using specific antibodies to one of the USP22 phosphorylation sites, T147, that is catalyzed by AKT ( xref )."
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"Unexpectedly, neither the expression levels of USP22, FOXO1, and ATGL nor USP22 phosphorylation show any statistically substantial increase in para-tumoral normal tissues (fig."
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