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10.1038/s41598-017-01614-6 http://scihub22266oqcxt.onion/10.1038/s41598-017-01614-6 C5431095!5431095!28469279     free     free     free Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Sci+Rep 2017 ; 7 (ä): ä Nephropedia Template TP {{tp|p=28469279|t=2017. Spindle pole cohesion requires glycosylation-mediated localization of NuMA |pdf=|usr=}}{{28469279}} gab.com Text Spindle pole cohesion requires glycosylation-mediated localization of NuMA JO: Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=28469279 #FOAvip Glycosylation is critical for the regulation of several cellular processes. One glycosylation pathway, the unusual O-linked ?-N-acetylglucosamine glycosylation (O-GlcNAcylation) has been shown to be required for proper mitosis, likely through a subset of proteins that are O-GlcNAcylated during metaphase. As lectins bind glycosylated proteins, we asked if specific lectins interact with mitotic O-GlcNAcylated proteins during metaphase to ensure correct cell division. Galectin-3, a small soluble lectin of the Galectin family, is an excellent candidate, as it has been previously described as a transient centrosomal component in interphase and mitotic epithelial cells. In addition, it has recently been shown to associate with basal bodies in motile cilia, where it stabilizes the microtubule-organizing center (MTOC). Using an experimental mouse model of chronic kidney disease and human epithelial cell lines, we investigate the role of Galectin-3 in dividing epithelial cells. Here we find that Galectin-3 is essential for metaphase where it associates with NuMA in an O-GlcNAcylation-dependent manner. We provide evidence that the NuMA-Galectin-3 interaction is important for mitotic spindle cohesion and for stable NuMA localization to the spindle pole, thus revealing that Galectin-3 is a novel contributor to epithelial mitotic progress. Twit Text FOAVip Spindle pole cohesion requires glycosylation-mediated localization of NuMA ????Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=28469279 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28469279 #FOAvip English Wikipedia <ref>{{Cite pmid|28469279}}</ref> Spindle pole cohesion requires glycosylation-mediated localization of NuMA #MMPMID28469279 Magescas J; Sengmanivong L; Viau A; Mayeux A; Dang T; Burtin M; Nilsson UJ; Leffler H; Poirier F; Terzi F; Delacour D Sci Rep 2017[]; 7 (ä): ä PMID28469279show ga Glycosylation is critical for the regulation of several cellular processes. One glycosylation pathway, the unusual O-linked ?-N-acetylglucosamine glycosylation (O-GlcNAcylation) has been shown to be required for proper mitosis, likely through a subset of proteins that are O-GlcNAcylated during metaphase. As lectins bind glycosylated proteins, we asked if specific lectins interact with mitotic O-GlcNAcylated proteins during metaphase to ensure correct cell division. Galectin-3, a small soluble lectin of the Galectin family, is an excellent candidate, as it has been previously described as a transient centrosomal component in interphase and mitotic epithelial cells. In addition, it has recently been shown to associate with basal bodies in motile cilia, where it stabilizes the microtubule-organizing center (MTOC). Using an experimental mouse model of chronic kidney disease and human epithelial cell lines, we investigate the role of Galectin-3 in dividing epithelial cells. Here we find that Galectin-3 is essential for metaphase where it associates with NuMA in an O-GlcNAcylation-dependent manner. We provide evidence that the NuMA-Galectin-3 interaction is important for mitotic spindle cohesion and for stable NuMA localization to the spindle pole, thus revealing that Galectin-3 is a novel contributor to epithelial mitotic progress. äSpindle pole cohesion requires glycosylation-mediated localization of (epmc).pdf DeepDyve Pubget Overpricing