Ubiquitous Importance of Protein Glycosylation

Methods Mol Biol. 2017;1503:1-12. doi: 10.1007/978-1-4939-6493-2_1.

Abstract

More than half of all proteins are glycosylated. The attached glycans provide proteins with important structural and functional properties and glycan parts of glycoproteins have essential roles in many key biological processes. This chapter describes the effect of glycosylation on the structure and function of proteins, with emphasis on regulation of protein half-life and modulation of protein function by alternative glycosylation. In addition, this chapter highlights the importance of glycan-lectin interactions, the ability of glycans to block phosphorylation of proteins, and the importance of glycans in disease.

Keywords: Alternative glycosylation; Glycans; Glycosylation in disease; IgG glycosylation; Lectins; O-GlcNAc; Protein function; Protein half-life; Protein structure.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Carbohydrate Sequence
  • Glycoproteins / chemistry
  • Glycoproteins / metabolism
  • Glycosylation
  • Humans
  • Immunoglobulin G / chemistry
  • Immunoglobulin G / metabolism
  • Lectins / chemistry
  • Lectins / metabolism
  • Phosphorylation
  • Polysaccharides / analysis*
  • Polysaccharides / metabolism
  • Protein Conformation
  • Protein Processing, Post-Translational
  • Proteins / chemistry*
  • Proteins / metabolism

Substances

  • Glycoproteins
  • Immunoglobulin G
  • Lectins
  • Polysaccharides
  • Proteins