IndraLab

Statements

USP24 is phosphorylated. 10 / 10
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"Phosphorylation of USP24 at these three residues was increased during mitosis ( xref )."
27991932
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"Three mutated residues and triple mutant S3A increased the USP24 level, suggesting that USP24 phosphorylation might be the reason for the decreased USP24 expression during mitosis and tumorigenesis."
27991932
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"We found that USP24 interacted with CDK1/cyclin B during the mitotic stage, and that the USP24 phosphorylation signal was higher in mitosis than in interphase ( xref ; xref )."
27991932
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"In addition, we found that USP24 phosphorylation at Ser2604 was declined by U0126, which inhibited the Erk1/2 activities in A549 cells ( xref ); however, USP24 phosphorylation was not decreased by LY294002, which inhibited the PI3K activities ( xref )."
27991932
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"Mutations at these residues increased the USP24 half-life during mitosis, suggesting that USP24 phosphorylation during mitosis decreased USP24 expression ( xref )."
27991932
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"In addition to the phosphorylation of USP24 in mitosis, USP24 is also phosphorylated by EGF-activated Erk1/2 kinase activity to turnover USP24."
27991932
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"Antibodies that recognized these phosphorylation residues were produced to study USP24 phosphorylation."
27991932
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"Phosphorylation of USP24 increases its degradation during tumorigenesis and cell cycle progression."
27991932
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"USP24 phosphorylation increased the recruitment of the E3 ligase cdc20, which is the subunit of the APC/C complex that provides the E3 ligase activity."
27991932
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"Here we found that the phosphorylation of several USP24 residues was regulated by EGF treatment and mitotic CDK1 to enhance USP24 degradation in a polyubiquitination-dependent manner."
27991932