Spindle pole cohesion requires glycosylation-mediated localization of NuMA

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Magescas, Jérémy | Sengmanivong, Lucie | Viau, Amandine | Mayeux, Adeline | Dang, Tien | Burtin, Martine | Nilsson, Ulf | Leffler, Hakon | Poirier, Françoise | Terzi, Fabiola | Delacour, Delphine

Edité par CCSD ; Nature Publishing Group -

International audience. 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.

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