IndraLab

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"Recently, CDK1 dependent phosphorylation of Usp16 on S552 was shown to promote an interaction between Usp16 and Plk1."

"To investigate this, we first set out to identify CDK1 phosphorylation sites on Usp16. By incubating GST-tagged Usp16 fragments, aa 1–150, aa 150–600, or aa 600–end individually with CDK1, we identified aa 150–600 as the only fragment being phosphorylated in vitro (Fig. 3 A). Sequence analysis revealed that S189 and S552 were potential phosphorylation sites for CDK1 (Fig. S2 A). Further analyses by in vitro phosphorylation assay and MS of peptides derived from proteins isolated from HeLa cells showed that S552 was the CDK1 phosphorylation site (Fig. S2, B and E), which was also reported recently (Xu et al., 2013). Next, we treated HeLa cells with CDK1 inhibitor RO3306 and observed a significant reduction in Plk1–Usp16 interaction (Fig. 3, C and E). Moreover, we found that only the WT GFP-Usp16, but not GFP-Usp16 S552A, could be coimmunoprecipitated with Plk1 from HeLa cell lysates (Fig. 3, D and F). These data strongly suggest that the phosphorylation of S552 by CDK1 promotes Plk1–Usp16 interaction."

"To investigate this, we first set out to identify CDK1 phosphorylation sites on Usp16. By incubating GST-tagged Usp16 fragments, aa 1–150, aa 150–600, or aa 600–end individually with CDK1, we identified aa 150–600 as the only fragment being phosphorylated in vitro (Fig. 3 A). Sequence analysis revealed that S189 and S552 were potential phosphorylation sites for CDK1 (Fig. S2 A). Further analyses by in vitro phosphorylation assay and MS of peptides derived from proteins isolated from HeLa cells showed that S552 was the CDK1 phosphorylation site (Fig."

"During mitosis, cyclin-dependent kinase 1 (Cdk1) phosphorylates USP16 at Ser552 and regulates its nuclear import by the exportin chromosome region maintenance 1 (Crm1) ( xref , xref )."

"Here, we report that cyclin-dependent kinase 1 (cdk1) phosphorylates the histone h2a deubiquitinase ubp-m at serine 552 (s552p), and, importantly, this phosphorylation is required for cell cycle progression."

"Ubp-M serine 552 phosphorylation by cyclin-dependent kinase 1 regulates cell cycle progression."