Function of N-glycosylation in Plants
A special issue of Plants (ISSN 2223-7747). This special issue belongs to the section "Plant Cell Biology".
Deadline for manuscript submissions: closed (31 December 2021) | Viewed by 413
Special Issue Editor
Special Issue Information
Dear Colleagues,
Glycoproteins are involved in diverse cellular mechanisms and glycobiology has become an important field in biology. In eukaryotic cells, asparagine-linked glycosylation (N-glycosylation) is one of the most common post-translational modifications for secreted proteins and membrane proteins, which are synthesized and folded in the endoplasmic reticulum (ER). It is known that N-glycosylation has various functions, represented by protein folding.
In plant science, researchers have made considerable progress in N-glycosylation research over the past few decades, and N-glycosylation has gradually turned out to be important in growth and stress resistance in plants. Perturbation in core N-glycosylation causes lethality, and has negative impacts on protein production. A lack of the genes in the complex N-glycan synthesis pathway causes increased salt stress sensitivity in Arabidopsis, as well as abnormal development and death before reproduction in rice. Besides this, N-glycosylation is an important topic in protein production, such as in vaccines for medical treatment in plant cell-based systems, because plants exhibit unique modifications on their complex N-glycans. Understanding the functions of N-glycosylation in plants will be useful in various fields in the future. This Special Issue broadly covers the latest achievements and progress made in plant N-glycosylation.
Dr. Yukihiro Nagashima
Guest Editor
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