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CK2 phosphorylates NPM1. 6 / 6
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"Interestingly, CIGB-300 was shown to bind NPM1 and to inhibit CK2-mediated phosphorylation of NPM1 at Ser125 inducing damage to the nucleolar architecture and massive apoptosis [149], in line with the putative implication of NPM1 phospho-Ser125 in the maintenance of the nucleolar assembly, in ribosome biogenesis, and in cytokinesis [153,154,155]."

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"During interphase, NPM1 has also been reported to be phosphorylated by casein kinase 2 (CK2) and this is thought to have a role in regulating the nucleolar structure by modulating the dynamic localization of NPM1 between nucleolus and nucleoplasm (Szebeni et al. 2003; Negi and Olson 2006)."
| PMC

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"Several laboratories have reported on CK2 phosphorylation of B23/nucleophosmin, including androgenic regulation, cell cycle regulation, and the impact on genes related to protein synthesis, energetic metabolism, and ribosomal biogenesis [122–126]."

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"Phosphorylation of Npm is catalyzed by CK2 and the cyclin dependent kinase cdc2 and cdk1."

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"Previous reports suggest that CKII kinase phosphorylates S125-NPM ( xref ; xref )."

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"As shown in Fig. 7, nucleophosmin and B23 was phosphorylated by CK2 associated with the cyclin H, cdk7, and Mat1 complex and this phosphorylation was completely inhibited by the CK2 specific substrate[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"