IndraLab

Statements

USP33 is phosphorylated. 11 / 11
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"The phosphorylated USP33 deubiquitinated arrestins locally, rather than globally, because USP33 specifically bound to arrestins associated with D 3 R and Mdm2 (Fig.  xref )."
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"CDK1-mediated phosphorylation of USP33 is pivotal for SIN1 stability and PDAC progression."
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"We next examined how CDK1-mediated phosphorylation of USP33 affects its ability to stabilize SIN1."
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"As shown in Fig. xref , phosphorylation of USP33 was detected in PANC-1 cells using a phospho-CDK substrate antibody."
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"A recent study revealed that AKT regulates the desensitization of D 2 -like receptors by phosphorylating the deubiquitinase USP33 [ xref ]."
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"The phosphorylated Akt subsequently phosphorylated USP33, which was recruited to the D 3 R under desensitization conditions (Figs. xref and xref )."
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"These results suggest that CDK1-mediated phosphorylation of USP33 is essential for its activity to regulating the ubiquitination and degradation of SIN1."
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"To assess the functional consequence of CDK1-mediated phosphorylation of USP33, we examined its role in SIN1-dependent malignant processes."
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"These results demonstrate that CDK1-mediated phosphorylation of USP33 is crucial for stabilizing SIN1 and promoting SIN1-dependent tumor progression in PDAC."
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"We show that CDK1-catalyzed phosphorylation of USP33 is a critical post-translational modification controlling SIN1 stability and its oncogenic activity."
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"Given that CDK1 phosphorylates USP33, which in turn stabilizes SIN1, we hypothesized that CDK1 might also regulate the stability and function of SIN1 in PDAC."
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