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10.1038/srep11777 http://scihub22266oqcxt.onion/10.1038/srep11777 C4485321!4485321 !26123729     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=26123729 &cmd=llinks): Failed to open stream: HTTP request failed! 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Cytoplasmic nucleophosmin has elevated T199 phosphorylation upon which G2/M phase progression is dependent |pdf=|usr=}}{{26123729 }} gab.com Text Cytoplasmic nucleophosmin has elevated T199 phosphorylation upon which G2/M phase progression is dependent JO: Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=26123729 #FOAvip The cytoplasmic mutant of nucleophosmin (NPMc) is found approximately in one-third of acute myeloid leukemia (AML) cases and is highly associated with normal karyotype. Whereas previous studies have focused on wtNPM in centrosome duplication, we further elucidate the role of NPM in the cell cycle by utilizing the increased cytoplasmic load of NPMc. Overexpression of NPMc causes increased phosphorylation of NPM on T199 and, to a lesser degree, S4. T199 phosphorylation is dependent on cdk2 but activators of cdk2 were not elevated. Upon inhibition of cdk2, NPMc-overexpressing cells demonstrate a greater G2/M phase arrest than wtNPM or GFP counterparts. However, the number of cells with 2 centrosomes did not increase concordantly. This suggests that the arrest was caused by a delay in centrosome duplication, most likely due to the inhibition of centrosome duplication caused by unphosphorylated NPMc. Overall, these results suggest that the phosphorylation of T199 is important in the mitotic progression of NPMc-expressing cells. This further supports the hypothesis that NPMc is associated with normal karyotypes in AML because the higher cytoplasmic load of NPM can better suppress centrosome overduplication which would otherwise result in unequal segregation of chromosomes during mitosis, leading to aneuploidy and other genomic instabilities. Twit Text FOAVip Cytoplasmic nucleophosmin has elevated T199 phosphorylation upon which G2/M phase progression is dependent ????Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=26123729 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26123729 #FOAvip English Wikipedia <ref>{{Cite pmid|26123729 }}</ref> Cytoplasmic nucleophosmin has elevated T199 phosphorylation upon which G2/M phase progression is dependent #MMPMID26123729 Chan N ; Lim TM Sci Rep 2015[Jun]; 5 (ä): 11777 PMID26123729 show ga The cytoplasmic mutant of nucleophosmin (NPMc) is found approximately in one-third of acute myeloid leukemia (AML) cases and is highly associated with normal karyotype. Whereas previous studies have focused on wtNPM in centrosome duplication, we further elucidate the role of NPM in the cell cycle by utilizing the increased cytoplasmic load of NPMc. Overexpression of NPMc causes increased phosphorylation of NPM on T199 and, to a lesser degree, S4. T199 phosphorylation is dependent on cdk2 but activators of cdk2 were not elevated. Upon inhibition of cdk2, NPMc-overexpressing cells demonstrate a greater G2/M phase arrest than wtNPM or GFP counterparts. However, the number of cells with 2 centrosomes did not increase concordantly. This suggests that the arrest was caused by a delay in centrosome duplication, most likely due to the inhibition of centrosome duplication caused by unphosphorylated NPMc. Overall, these results suggest that the phosphorylation of T199 is important in the mitotic progression of NPMc-expressing cells. This further supports the hypothesis that NPMc is associated with normal karyotypes in AML because the higher cytoplasmic load of NPM can better suppress centrosome overduplication which would otherwise result in unequal segregation of chromosomes during mitosis, leading to aneuploidy and other genomic instabilities. |Centrosome/metabolism [MESH] |Cyclin-Dependent Kinase 2/metabolism [MESH] |Cytoplasm [MESH] |Enzyme Activation [MESH] |G2 Phase [MESH] |HEK293 Cells [MESH] |Humans [MESH] |Leukemia, Myeloid, Acute [MESH] |Mutation, Missense [MESH] |Nuclear Proteins/genetics/*metabolism [MESH] |Nucleophosmin [MESH] |Phosphorylation [MESH] |Protein Processing, Post-Translational [MESH] |Protein Transport [MESH]Cytoplasmic nucleophosmin has elevated T199 phosphorylation upon which(epmc).pdf DeepDyve Pubget Overpricing