IndraLab

"We also demonstrated for the first time that PPM1D up-regulated phosphorylation of Thr199 and Ser4 of NPM sequentially via the CDC25C-CDK1-PLK1 signalling cascade thereby modulating nucleolar formation (Fig. 6). While phosphorylation at Thr199 by CDK1 and Ser4 by PLK1 has been reported in separate studies27383940, an association between these sites has not previously been reported. Our results suggested that phosphorylation of Thr199 by CDK1 was important for phosphorylation of Ser4 by PLK1."

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"It is suggested that phosphorylation of Thr199 of NPM by CDK1 enhances phosphorylation of Ser4 of NPM by PLK1."

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"Phosphorylated at ser-4 by plk1 and plk2. Phosphorylation at ser-4 by plk2 in s phase is required for centriole duplication and is sufficient to trigger centriole replication. Phosphorylation at ser-4 by plk1 takes place during mitosis."

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"An in vitro kinase assay showed that phosphorylated-NPM at Thr199 by CDK1 enhanced NPM phosphorylation at Ser4 by PLK1 as revealed by Western blotting with the phospho-specific NPM antibodies (Fig. 5a)."

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"In this report, we showed that phosphorylation of NPM by CDK1 including Thr199 induces sequential phosphorylation of Ser4 by PLK1. We also demonstrated that PPM1D is an upstream regulator of the CDC25C-CDK1-PLK1 cascade and controls the phosphorylation level of NPM. Furthermore, we show for the first time that sequential phosphorylation of NPM at Thr199 and Ser4 is important for regulating nucleolar formation."

"An in vitro kinase assay showed that phosphorylated-NPM at Thr199 by CDK1 enhanced NPM phosphorylation at Ser4 by PLK1 as revealed by Western blotting with the phospho-specific NPM antibodies ( xref )."

"An in vitro kinase assay showed that phosphorylated-NPM at Thr199 by CDK1 enhanced NPM phosphorylation at Ser4 by PLK1 as revealed by Western blotting with the phospho specific NPM antibodies (XREF_FIG)."

"We also demonstrated for the first time that PPM1D up-regulated phosphorylation of Thr199 and Ser4 of NPM sequentially via the CDC25C-CDK1-PLK1 signalling cascade thereby modulating nucleolar formation (Fig. 6). While phosphorylation at Thr199 by CDK1 and Ser4 by PLK1 has been reported in separate studies27383940, an association between these sites has not previously been reported. Our results suggested that phosphorylation of Thr199 by CDK1 was important for phosphorylation of Ser4 by PLK1. Phosphorylation at Thr199 by CDK1 was suggested to be involved in dissociation of NPM from the centrosome, leading to centrosome duplication40, and in regulation of RNA binding activity of NPM3839. Phosphorylation at Ser4 by PLK1 was reported to be involved in regulation of mitosis27."

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