Spindle pole cohesion requires glycosylation-mediated localization of NuMA

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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 Magescas
  • Lucie Sengmanivong
  • Amandine Viau
  • Adeline Mayeux
  • Tien Dang
  • Martine Burtin
  • Ulf Nilsson
  • Hakon Leffler
  • Françoise Poirier
  • Fabiola Terzi
  • Delphine Delacour
Enheter & grupper
Externa organisationer
  • Curie Institute, Paris
  • Paris Descartes University
  • Paris Diderot University

Ämnesklassifikation (UKÄ) – OBLIGATORISK

  • Cell- och molekylärbiologi
  • Cellbiologi
TidskriftScientific Reports
StatusPublished - 2017 dec 1
Peer review utfördJa