期刊
FRONTIERS IN PLANT SCIENCE
卷 5, 期 -, 页码 -出版社
FRONTIERS RESEARCH FOUNDATION
DOI: 10.3389/fpls.2014.00363
关键词
endoplasmic reticulum; Golgi apparatus; protein glycosylation; N-glycosylation; glycoprotein; N-acetylglucosaminyltransferase
资金
- Austrian Science Fund (FWF) [P23906-B20]
- Austrian Science Fund (FWF) [P 23906] Funding Source: researchfish
- Austrian Science Fund (FWF) [P23906] Funding Source: Austrian Science Fund (FWF)
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 beta 1,2-xylose, core alpha l,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.
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