Galectin Lattice Regulates Nutrition Sensor Functions in Pancreatic β Cells

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Author(s)

    • Maeda Kento
    • Department of Analytical Biochemistry, Graduate School of Health Sciences, Kumamoto University
    • Ohtsubo Kazuaki
    • Department of Analytical Biochemistry, Graduate School of Health Sciences, Kumamoto University|Department of Analytical Biochemistry, Faculty of Life Sciences, Kumamoto University

Abstract

<p>Recently, it has been elucidated that the lattice structure formed by complexes of galectins and <i>N</i>-glycans regulates expression and function of plasmalemmal glycoproteins, which is important for maintaining various homeostatic systems. We have previously revealed that the failure of <i>N</i>-glycosylation abolishes lattice formation and induces aberrant membrane sub-domain distribution of Glucose transporter 2 (GLUT2) in pancreatic β cells that consequently attenuates the cellular glucose uptake function. This results in the impairment of insulin secretion in pancreatic β cells in the disease process of diabetes. Although the biological significance of the formation of the galectin lattice is well recognized, the molecular regulatory mechanism of the localization and function of plasmalemmal glycoproteins has not been clarified. To address the question, we analyzed the component proteins of the galectin lattice complexes on pancreatic β cell surface and found that the lattice complexes were composed of Cationic amino acid transporter 3 (CAT3), Teneurin-3, Myosin-4, Actin, α-Tubulin, and GLUT2 at least. These results indicated that the galectin lattice forms clusters of plasmalemmal glycoproteins through galectin-<i>N</i>-glycan bindings and further suggested the presence of the common mechanism among the functional regulation of nutrition sensors in the insulin secretion of pancreatic β cells.</p>

Journal

  • Trends in Glycoscience and Glycotechnology

    Trends in Glycoscience and Glycotechnology 31(178), E27-E29, 2019

    FCCA(Forum: Carbohydrates Coming of Age)

Codes

  • NII Article ID (NAID)
    130007556943
  • Text Lang
    ENG
  • ISSN
    0915-7352
  • Data Source
    J-STAGE 
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