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Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions
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The galectin lattice at a glance.

Ivan R Nabi1, Jay Shankar2, James W Dennis3

  • 1Department of Cellular and Physiological Sciences, Life Sciences Institute, 2350 Health Sciences Mall, University of British Columbia, Vancouver, British Columbia, Canada V6T 1Z3 irnabi@mail.ubc.ca dennis@lunenfeld.ca.

Journal of Cell Science
|June 21, 2015
PubMed
Summary

Galectins form dynamic lattices that regulate cell surface molecules and T cell functions. Their binding affinity depends on N-glycan branching, offering insights into lectin and glycome biology.

Keywords:
EndocytosisGalectinGlycolipidGlycosylationMGATsReceptor

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Glycobiology

Background:

  • Galectins are beta-galactoside-binding lectins widely expressed in metazoans.
  • Mammalian galectins, characterized by conserved carbohydrate recognition domains (CRDs), form dynamic lattices that regulate cell surface processes.
  • Galectin-3 exhibits pentamerization, contributing to lattice structure and function.

Purpose of the Study:

  • To elucidate the regulatory role of the galectin lattice in cell membrane dynamics and cellular processes.
  • To investigate the relationship between N-glycan structure and galectin lattice affinity.
  • To explore the potential of galectin-ligand interactions for analyzing lectin and glycome functions.

Main Methods:

  • The study focuses on the structural and functional aspects of galectin lattices.
  • Analysis of N-glycan branching mediated by Golgi N-acetylglucosaminyltransferase-branching enzymes.
  • Examination of UDP-GlcNAc supply via the hexosamine biosynthesis pathway.

Main Results:

  • The galectin lattice controls the diffusion, compartmentalization, and endocytosis of plasma membrane glycoproteins and glycolipids.
  • It regulates T cell selection, activation, and arrest, as well as signaling pathways and membrane receptor functionality.
  • Transmembrane glycoprotein affinity for the galectin lattice is directly proportional to N-glycan number and branching.

Conclusions:

  • Galectin lattices are crucial regulators of cell surface organization and function.
  • N-glycan branching, influenced by Golgi enzymes and metabolic flux, dictates glycoprotein affinity for galectins.
  • This interaction provides a framework for understanding lectin and broader glycome biological roles.