Phosphorylation of multifunctional nucleolar protein nucleophosmin (NPM1) by aurora kinase B is critical for mitotic progression
| Autor: | Tapas K. Kundu, Jayasha Shandilya, Karthigeyan Dhanasekaran, Parijat Senapati, Manoj Kumar, Gopinath S. Kodaganur, A. Hari Kishore, Suma S. Bangalore, Akshay Bhat |
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| Rok vydání: | 2013 |
| Předmět: |
Biophysics
Aurora inhibitor Aurora B kinase Mitosis macromolecular substances Serine threonine protein kinase Biology Biochemistry Mice Aurora kinase Structural Biology Genetics Animals Aurora Kinase B Humans Centrosome duplication Telophase Phosphorylation Molecular Biology Cytokinesis Aurora Kinase A Centrosome Nuclear Proteins Cell Biology Aurora kinases Cell biology enzymes and coenzymes (carbohydrates) Midbody Spindle checkpoint Protein Transport Cell Transformation Neoplastic HEK293 Cells embryonic structures Cancer research Carcinoma Squamous Cell NIH 3T3 Cells Mouth Neoplasms biological phenomena cell phenomena and immunity Nucleophosmin Protein Processing Post-Translational |
| Zdroj: | FEBS letters. 588(14) |
| ISSN: | 1873-3468 |
| Popis: | The functional association of NPM1 with Aurora kinases is well documented. Surprisingly, although NPM1 is a well characterized phosphoprotein, it is unknown whether it is a substrate of Aurora kinases. We have found that Aurora kinases A and B can phosphorylate NPM1 at a single serine residue, Ser125, in vitro and in vivo. Phosphorylated-S125-NPM1 (pS125-NPM1) localizes to the midbody region during late cytokinesis where it colocalizes with Aurora B. The overexpression of mutant (S125A) NPM1 resulted in the deregulation of centrosome duplication and mitotic defects possibly due to cytokinesis failure. These data suggest that Aurora kinase B-mediated phosphorylation of NPM1 plays a critical role during mitosis, which could have wider implications in oncogenesis. |
| Databáze: | OpenAIRE |
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