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.
CITATION STYLE
Schoberer, J., Shin, Y. J., Vavra, U., Veit, C., & Strasser, R. (2018). Analysis of protein glycosylation in the ER. In Methods in Molecular Biology (Vol. 1691, pp. 205–222). Humana Press Inc. https://doi.org/10.1007/978-1-4939-7389-7_16
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