Spindle pole cohesion requires glycosylation-mediated localization of NuMA

Abstract Glycosylation is critical for the regulation of several cellular processes. One glycosylation pathway, the unusual O-linked β-N-acetylglucosamine glycosylation (O-GlcNAcylation) has been shown to be required for proper mitosis, likely through a subset of proteins that are O-GlcNAcylated dur...

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Autores principales:	Jérémy Magescas, Lucie Sengmanivong, Amandine Viau, Adeline Mayeux, Tien Dang, Martine Burtin, Ulf J. Nilsson, Hakon Leffler, Françoise Poirier, Fabiola Terzi, Delphine Delacour
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/c6d69700b2e14178b5342c6ead7e8f61
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spelling	oai:doaj.org-article:c6d69700b2e14178b5342c6ead7e8f612021-12-02T11:40:33ZSpindle pole cohesion requires glycosylation-mediated localization of NuMA10.1038/s41598-017-01614-62045-2322https://doaj.org/article/c6d69700b2e14178b5342c6ead7e8f612017-05-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-01614-6https://doaj.org/toc/2045-2322Abstract Glycosylation is critical for the regulation of several cellular processes. One glycosylation pathway, the unusual O-linked β-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.Jérémy MagescasLucie SengmanivongAmandine ViauAdeline MayeuxTien DangMartine BurtinUlf J. NilssonHakon LefflerFrançoise PoirierFabiola TerziDelphine DelacourNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-14 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Jérémy Magescas Lucie Sengmanivong Amandine Viau Adeline Mayeux Tien Dang Martine Burtin Ulf J. Nilsson Hakon Leffler Françoise Poirier Fabiola Terzi Delphine Delacour Spindle pole cohesion requires glycosylation-mediated localization of NuMA
description	Abstract Glycosylation is critical for the regulation of several cellular processes. One glycosylation pathway, the unusual O-linked β-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.
format	article
author	Jérémy Magescas Lucie Sengmanivong Amandine Viau Adeline Mayeux Tien Dang Martine Burtin Ulf J. Nilsson Hakon Leffler Françoise Poirier Fabiola Terzi Delphine Delacour
author_facet	Jérémy Magescas Lucie Sengmanivong Amandine Viau Adeline Mayeux Tien Dang Martine Burtin Ulf J. Nilsson Hakon Leffler Françoise Poirier Fabiola Terzi Delphine Delacour
author_sort	Jérémy Magescas
title	Spindle pole cohesion requires glycosylation-mediated localization of NuMA
title_short	Spindle pole cohesion requires glycosylation-mediated localization of NuMA
title_full	Spindle pole cohesion requires glycosylation-mediated localization of NuMA
title_fullStr	Spindle pole cohesion requires glycosylation-mediated localization of NuMA
title_full_unstemmed	Spindle pole cohesion requires glycosylation-mediated localization of NuMA
title_sort	spindle pole cohesion requires glycosylation-mediated localization of numa
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/c6d69700b2e14178b5342c6ead7e8f61
work_keys_str_mv	AT jeremymagescas spindlepolecohesionrequiresglycosylationmediatedlocalizationofnuma AT luciesengmanivong spindlepolecohesionrequiresglycosylationmediatedlocalizationofnuma AT amandineviau spindlepolecohesionrequiresglycosylationmediatedlocalizationofnuma AT adelinemayeux spindlepolecohesionrequiresglycosylationmediatedlocalizationofnuma AT tiendang spindlepolecohesionrequiresglycosylationmediatedlocalizationofnuma AT martineburtin spindlepolecohesionrequiresglycosylationmediatedlocalizationofnuma AT ulfjnilsson spindlepolecohesionrequiresglycosylationmediatedlocalizationofnuma AT hakonleffler spindlepolecohesionrequiresglycosylationmediatedlocalizationofnuma AT francoisepoirier spindlepolecohesionrequiresglycosylationmediatedlocalizationofnuma AT fabiolaterzi spindlepolecohesionrequiresglycosylationmediatedlocalizationofnuma AT delphinedelacour spindlepolecohesionrequiresglycosylationmediatedlocalizationofnuma
_version_	1718395605632417792

Spindle pole cohesion requires glycosylation-mediated localization of NuMA

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