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Phosphorylation of multifunctional nucleolar protein nucleophosmin (NPM1) by aurora kinase B is critical for mitotic progression
Author(s) -
Shandilya Jayasha,
Senapati Parijat,
Dhanasekaran Karthigeyan,
Bangalore Suma S.,
Kumar Manoj,
Hari Kishore A.,
Bhat Akshay,
Kodaganur Gopinath S.,
Kundu Tapas K.
Publication year - 2014
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2014.05.014
Subject(s) - microbiology and biotechnology , midbody , aurora inhibitor , cytokinesis , aurora a kinase , mitosis , phosphorylation , kinase , biology , aurora b kinase , aurora kinase , nucleophosmin , npm1 , cancer research , chemistry , biochemistry , cell cycle , cell , cell division , gene , karyotype , chromosome , myeloid leukemia
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.