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

Endoglycosidase and glycoamidase release of N-linked glycans.

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1
Sanford-Burnham Medical Research Institute, La Jolla, California, USA.

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.

PMID:
21104982
DOI:
10.1002/0471140864.ps1204s62
[Indexed for MEDLINE]
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