Structure, biosynthesis, and function of asparagine-linked glycans on plant glycoproteins |
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Authors: | Loï c Faye,Kenneth D. Johnson,Arnd Sturm,Maarten J. Chrispeels |
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Affiliation: | CNRS –UA 203 –Facultédes Sciences de Rouen-F-76130 Mont-Saint-Aignan, France;Dept. of Biology, San Diego Slate Univ., San Diego, CA 92182, USA;A. Sturm and M. J. Chrispeels, Dept. of Biology, Univ. of California, San Diego, La Jolla, CA 92093-0016, USA. |
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Abstract: | In plants, glycoproteins with asparagine-linked glycans (oligosaccharides) are found in vacuoles, in the extracellular space or matrix, and associated with the endo-membrane system (endoplasmic reticulum, Golgi apparatus, plasma membrane, tonoplast). These glycans are of the high-mannose type, with a structure identical to that found in other organisms (mammals, yeast), or of the complex type with a β1–2 linked xylosyl residue not found in mammalian complex glycans. Asparagine-linked glycans play multiple roles by modifying the physicochemical properties of the polypeptides to which they are attached. |
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Keywords: | Asparagine-linked glycans complex glycans endoplasmic reticulum Golgi complex high-mannose glycans |
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