ArticleScientific reports2017
Spindle pole cohesion requires glycosylation-mediated localization of NuMA.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 30 citations in OpenAlex.
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- Intracellular galectin interactions in health and disease.Seminars in immunopathology · 2024Review
- Targeting disordered-structured domain interactions in Galectin-3 based on NMR and enhanced MD.Biophysical journal · 2022Article
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- Overcoming Microenvironment-Mediated Chemoprotection through Stromal Galectin-3 Inhibition in Acute Lymphoblastic Leukemia.International journal of molecular sciences · 2021Article
- Increased Circulating Levels of Galectin Proteins in Patients with Breast, Colon, and Lung Cancer.Cancers · 2021Article
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- The Emerging Role of Galectins andCells · 2020Review
- Galectin-3 in Inflammasome Activation and Primary Biliary Cholangitis Development.International journal of molecular sciences · 2020Review
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- Galectin-3 modulates epithelial cell adaptation to stress at the ER-mitochondria interface.Cell death & disease · 2020Article
- Centrosomes: Til O-GlcNAc Do Us Apart.Frontiers in endocrinology · 2020Review
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- Messenger RNA Life-Cycle in Cancer Cells: Emerging Role of Conventional and Non-Conventional RNA-Binding Proteins?International journal of molecular sciences · 2018Review
- O-GlcNAc: A Sweetheart of the Cell Cycle and DNA Damage Response.Frontiers in endocrinology · 2018Review
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- The nuclear mitotic apparatus protein NuMA controls rDNA transcription and mediates the nucleolar stress response in a p53-independent manner.Nucleic acids research · 2017Article
Corrections and comments
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Authors and funding
11 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
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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