Endoglycosidase and glycoamidase release of N-linked glycans

Curr Protoc Mol Biol. 2010 Jan:Chapter 17:Unit 17.13A. doi: 10.1002/0471142727.mb1713as89.

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 traffics from the ER to the Golgi toward its final location.

MeSH terms

  • Amidohydrolases / metabolism*
  • Animals
  • Chemistry Techniques, Analytical / methods*
  • Glycoproteins / analysis*
  • Glycoproteins / chemistry
  • Glycoproteins / metabolism*
  • Glycoside Hydrolases / metabolism*
  • Humans
  • Polysaccharides / analysis*
  • Polysaccharides / chemistry
  • Polysaccharides / metabolism
  • Protein Processing, Post-Translational*

Substances

  • Glycoproteins
  • Polysaccharides
  • Glycoside Hydrolases
  • Amidohydrolases