{Reference Type}: Journal Article
{Title}: Analysis of Protein Glycosylation in the ER.
{Author}: Schoberer J;Shin YJ;Vavra U;Veit C;Strasser R;
{Journal}: Methods Mol Biol
{Volume}: 2772
{Issue}: 0
{Year}: 2024
暂无{DOI}: 10.1007/978-1-0716-3710-4_16
{Abstract}: Protein N-glycosylation is an essential posttranslational modification which is initiated in the endoplasmic reticulum (ER). In plants, the N-glycans play a pivotal role in 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.