Endoglycosidase and glycoamidase release of N-linked glycans.
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.
Freeze
Hudson H
HH
Burnham Institute for Medical Research, La Jolla, California, USA.
Kranz
Christian
C
D000581:Amidohydrolases / Q000378:metabolism*; D000818:Animals; D002623:Chemistry Techniques, Analytical / Q000379:methods*; D006023:Glycoproteins / Q000032:analysis* / Q000737:chemistry / Q000378:metabolism*; D006026:Glycoside Hydrolases / Q000378:metabolism*; D006801:Humans; D011134:Polysaccharides / Q000032:analysis* / Q000737:chemistry / Q000378:metabolism; D011499:Protein Processing, Post-Translational
D006023:Glycoproteins; D011134:Polysaccharides; D006026:Glycoside Hydrolases; D000581:Amidohydrolases