Manipulating cell surface glycoproteins by targeting N-glycan-galectin interactions

Abstract

The interaction of cell surface receptors and transporters with cognate ligands depends on their concentration, distribution, and organization at the cellular surface. The majority of cell surface receptors and transporters are co- and/or post-translationally modified with asparagine (N)-linked oligosaccharides (glycans). N-Glycan number and structure combine to control the concentration of glycoproteins at the cell surface through interactions with endogenous lectins such as galectins. ER/Golgi enzyme activity and hexosamine pathway supply of Golgi metabolites co-dependently regulate N-glycan biosynthesis and combine to provide adaptive control over cell growth and differentiation. Studies in mice and humans have revealed metabolic and genetic dysregulation of N-glycosylation in T-cell-mediated autoimmunity. In this chapter, we describe methods used to analyze N-glycan-galectin interactions in controlling the distribution and organization of cell surface receptors and transporters.