title: Plant protein glycosylation.
abstract: Protein glycosylation is an essential co- and post-translational modification of secretory and membrane proteins in all eukaryotes. The initial steps of N-glycosylation and N-glycan processing are highly conserved between plants, mammals and yeast. In contrast, late N-glycan maturation steps in the Golgi differ significantly in plants giving rise to complex N-glycans with β1,2-linked xylose, core α1,3-linked fucose and Lewis A-type structures. While the essential role of N-glycan modifications on distinct mammalian glycoproteins is already well documented, we have only begun to decipher the biological function of this ubiquitous protein modification in different plant species. In this review, I focus on the biosynthesis and function of different protein N-linked glycans in plants. Special emphasis is given on glycan-mediated quality control processes in the ER and on the biological role of characteristic complex N-glycan structures.
authors.affiliation: Department of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Vienna, Muthgasse 18, 1190 Vienna, Austria richard.strasser@boku.ac.at.
authors.forename: Richard
authors.initials: R
authors.lastname: Strasser
mesh_terms: D000818:Animals; D017360:Arabidopsis / Q000378:metabolism; D006023:Glycoproteins / Q000235:genetics / Q000378:metabolism*; D006031:Glycosylation; D006056:Golgi Apparatus / Q000378:metabolism; D008322:Mammals / Q000378:metabolism; D010940:Plant Proteins / Q000235:genetics / Q000378:metabolism*; D011134:Polysaccharides / Q000096:biosynthesis* / Q000378:metabolism; D011499:Protein Processing, Post-Translational / Q000235:genetics*; D014994:Xylose / Q000235:genetics / Q000378:metabolism; D015003:Yeasts / Q000378:metabolism
chemical_list: D006023:Glycoproteins; D010940:Plant Proteins; D011134:Polysaccharides; D014994:Xylose
keywords: Golgi apparatus; N-glycan processing; N-glycosylation; endoplasmic reticulum; glycosyltransferase