Endoglycosidase and glycoamidase release of N-linked glycans

Curr Protoc Protein Sci. 2010 Nov:Chapter 12:Unit12.4. doi: 10.1002/0471140864.ps1204s62.

Abstract

Nearly all proteins entering the lumen of the endoplasmic reticulum (ER) become glycosylated en route to a cellular organelle, the plasma membrane, or the extracellular space. Many glycans can be attached to proteins, but the most common are the N-linked glycans (oligosaccharides). These chains are added very soon after a protein enters the ER, but they undergo extensive remodeling (processing), especially in the Golgi. Processing changes the sensitivity of the N-glycan to enzymes that cleave entire sugar chains or individual monosaccharides, which also changes the migration of the protein on SDS gels. These changes can be used to indicate when a protein has passed a particular subcellular location. This unit details some of the methods used to track a protein as it trafficks from the ER to the Golgi toward its final location.

MeSH terms

  • Chemistry Techniques, Analytical*
  • Electrophoresis, Polyacrylamide Gel / methods
  • Electrophoretic Mobility Shift Assay / methods
  • Endoplasmic Reticulum / metabolism
  • Glucan 1,4-alpha-Glucosidase / metabolism*
  • Glycoside Hydrolases / metabolism*
  • Glycosylation
  • Golgi Apparatus / metabolism
  • Neuraminidase / metabolism
  • Oligosaccharides / chemistry*
  • Oligosaccharides / metabolism*
  • Protein Processing, Post-Translational
  • Proteins / chemistry
  • Proteins / metabolism*

Substances

  • Oligosaccharides
  • Proteins
  • Glycoside Hydrolases
  • Neuraminidase
  • Glucan 1,4-alpha-Glucosidase