IndraLab

Statements


CDK1 phosphorylates USP22. 15 / 27
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sparser
"Phosphorylation of USP22 by CDK1 enhances its activity in deubiquitinating CCNB1."

sparser
"CDK1 phosphorylates USP22 to optimize its activity in CCNB1 stabilization during the G2/M phase."

sparser
"From our proteomic analysis, we noticed that CCNB1 appears to form a complex with both USP22 and CDK1; this prompted us to ask whether CDK1 phosphorylates USP22."

sparser
"We then analyzed whether USP22 is phosphorylated by CDK1."

sparser
"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 )."

reach
"Phosphorylation of USP22 by CDK1 enhances its activity in deubiquitinating CCNB1."

reach
"CDK1 phosphorylates USP22 to optimize its activity in CCNB1 stabilization during the G2/M phase."

reach
"From our proteomic analysis, we noticed that CCNB1 appears to form a complex with both USP22 and CDK1; this prompted us to ask whether CDK1 phosphorylates USP22."

reach
"We then analyzed whether USP22 is phosphorylated by CDK1."

reach
"In addition, expression of the constitutively active form of CDK1 (CDK1/AF) [XREF_BIBR, XREF_BIBR] further enhanced USP22 phosphorylation in HCT116 cells (XREF_FIG)."

reach
"CDK1 phosphorylates USP22 to enhance its activity in CCNB1 stabilization during G2/M phase."

sparser
"CDK1 phosphorylates USP22 to enhance its activity in CCNB1 stabilization during G2/M phase."

reach
"Third, USP22 is phosphorylated by CDK1 during the G2/M phase of the cell cycle and this phosphorylation optimizes the enzyme activity of USP22 to deubiquitinate CCNB1."

reach
"Interestingly, USP22 activity is regulated by CDK1, which catalyzes USP22 phosphorylation to elevate USP22 ability in CCNB1 deubiquitination and stabilization."

sparser
"Interestingly, USP22 is also phosphorylated by CDK1, and this phosphorylation enhances its activity in deubiquitinating cyclin B1."