Chapter title |
The Use of Glycosylation Tags as Reporters for Protein Entry into the Endoplasmic Reticulum in Yeast and Mammalian Cells.
|
---|---|
Chapter number | 21 |
Book title |
Peroxisomes
|
Published in |
Methods in molecular biology, January 2017
|
DOI | 10.1007/978-1-4939-6937-1_21 |
Pubmed ID | |
Book ISBNs |
978-1-4939-6935-7, 978-1-4939-6937-1
|
Authors |
Buentzel, Judith, Thoms, Sven, Judith Buentzel, Sven Thoms |
Editors |
Michael Schrader |
Abstract |
N-glycosylation is a process occurring in the Endoplasmic Reticulum (ER) in nearly every organism. Proteins containing a glycosylation site are quickly glycosylated by oligosaccharyltransferases once the glycosylation site is exposed to the ER lumen. The oligosaccharide tree is then modified and proteins are targeted to specific organelles or subcompartments. For a long time peroxisomal membrane proteins (PMP) were thought to be targeted directly to the peroxisome. However, in the course of recent years, several PMPs were found to be targeted via the ER. Glycosylation increases the molecular weight of a protein, which is easily detected by Western blotting. Glycosylation tags like the opsin tag are therefore useful tools in the study of ER entry of peroxisomal proteins. |
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