Chapter title |
Analysis of Protein Glycosylation in the ER
|
---|---|
Chapter number | 16 |
Book title |
The Plant Endoplasmic Reticulum
|
Published in |
Methods in molecular biology, January 2018
|
DOI | 10.1007/978-1-4939-7389-7_16 |
Pubmed ID | |
Book ISBNs |
978-1-4939-7388-0, 978-1-4939-7389-7
|
Authors |
Jennifer Schoberer, Yun-Ji Shin, Ulrike Vavra, Christiane Veit, Richard Strasser, Schoberer J, Shin YJ, Vavra U, Veit C, Strasser R, Schoberer, Jennifer, Shin, Yun-Ji, Vavra, Ulrike, Veit, Christiane, Strasser, Richard |
Abstract |
Protein N-glycosylation is an essential posttranslational modification which is initiated in the endoplasmic reticulum. In plants, the N-glycans play a pivotal role for protein folding and quality control. Through the interaction of glycan processing and binding reactions mediated by ER-resident glycosidases and specific carbohydrate binding proteins, the N-glycans contribute to the adoption of a native protein conformation. Properly folded glycoproteins are released from these processes and allowed to continue their transit to the Golgi where further processing and maturation of N-glycans leads to the formation of more complex structures with different functions. Incompletely folded glycoproteins are removed from the ER by a highly conserved degradation process to prevent the accumulation or secretion of misfolded proteins and maintain ER homeostasis. Here, we describe methods to analyze the N-glycosylation status and the glycan-dependent ER-associated degradation process in plants. |
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