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Phosphorylation of multifunctional nucleolar protein nucleophosmin (NPM1) by aurora kinase B is critical for mitotic progression

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dc.contributor.author Shandilya, Jayasha
dc.contributor.author Senapati, Parijat
dc.contributor.author Dhanasekaran, Karthigeyan
dc.contributor.author Bangalore, Suma S.
dc.contributor.author Kumar, Manoj
dc.contributor.author Kishore, A. Hari
dc.contributor.author Bhat, Akshay
dc.contributor.author Kodaganur, Gopinath S.
dc.contributor.author Kundu, Tapas Kumar
dc.date.accessioned 2017-02-17T05:09:15Z
dc.date.available 2017-02-17T05:09:15Z
dc.date.issued 2014
dc.identifier.citation Shandilya, J; Senapati, P; Dhanasekaran, K; Bangalore, SS; Kumar, M; Kishore, AH; Bhat, A; Kodaganur, GS; Kundu, TK, Phosphorylation of multifunctional nucleolar protein nucleophosmin (NPM1) by aurora kinase B is critical for mitotic progression. Febs Letters 2014, 588 (14) 2198-2205, http://dx.doi.org/10.1016/j.febslet.2014.05.014 en_US
dc.identifier.citation EBS Letters en_US
dc.identifier.citation 588 en_US
dc.identifier.citation 14 en_US
dc.identifier.issn 0014-5793
dc.identifier.uri https://libjncir.jncasr.ac.in/xmlui/10572/2326
dc.description Restricted Access en_US
dc.description.abstract The functional association of NPM1 with Aurora ldnases 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 cytoldnesis 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. Structured summary of protein interactions: Aurora A phosphorylates NPM by protein kinase assay (1,2) Aurora B phosphorylates NPM by protein kinase assay (View interaction) NPM and Aurora A colocalize by fluorescence microscopy (View interaction) NPM and Aurora B colocalize by fluorescence microscopy (View interaction) NPM binds to Aurora B by pull down (View interaction) NPM physically interacts with Aurora B by anti tag coimmunoprecipitation (1,2) (C) 2014 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. en_US
dc.description.uri 1873-3468 en_US
dc.description.uri http://dx.doi.org/10.1016/j.febslet.2014.05.014 en_US
dc.language.iso English en_US
dc.publisher Elsevier Science Bv en_US
dc.rights @Elsevier Science Bv, 2014 en_US
dc.subject Biochemistry & Molecular Biology en_US
dc.subject Biophysics en_US
dc.subject Cell Biology en_US
dc.subject Aurora Kinases en_US
dc.subject Nucleophosmin en_US
dc.subject Mitosis en_US
dc.subject Cytokinesis en_US
dc.subject Phosphorylation en_US
dc.subject Serine Threonine Protein Kinase en_US
dc.subject Centrosome Duplication en_US
dc.subject Histone Chaperone en_US
dc.subject Dependent Kinase en_US
dc.subject Oral-Cancer en_US
dc.subject Transcription en_US
dc.subject Activation en_US
dc.subject Expression en_US
dc.subject Target en_US
dc.title Phosphorylation of multifunctional nucleolar protein nucleophosmin (NPM1) by aurora kinase B is critical for mitotic progression en_US
dc.type Article en_US


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