title: Biological significance of complex N-glycans in plants and their impact on plant physiology.
abstract: Asparagine (N)-linked protein glycosylation is a ubiquitous co- and post-translational modification which can alter the biological function of proteins and consequently affects the development, growth, and physiology of organisms. Despite an increasing knowledge of N-glycan biosynthesis and processing, we still understand very little about the biological function of individual N-glycan structures in plants. In particular, the N-glycan-processing steps mediated by Golgi-resident enzymes create a structurally diverse set of protein-linked carbohydrate structures. Some of these complex N-glycan modifications like the presence of β1,2-xylose, core α1,3-fucose or the Lewis a-epitope are characteristic for plants and are evolutionary highly conserved. In mammals, complex N-glycans are involved in different cellular processes including molecular recognition and signaling events. In contrast, the complex N-glycan function is still largely unknown in plants. Here, in this short review, I focus on important recent developments and discuss their implications for future research in plant glycobiology and plant biotechnology.
authors.affiliation: Department of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences Vienna, Austria.
authors.forename: Richard
authors.initials: R
authors.lastname: Strasser
keywords: Golgi apparatus; N-acetylglucosaminyltransferase; N-glycosylation; endoplasmic reticulum; glycoprotein; protein glycosylation
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