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Plant protein glycosylation
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...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Oxford University Press
2016
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5045529/ https://www.ncbi.nlm.nih.gov/pubmed/26911286 http://dx.doi.org/10.1093/glycob/cww023 |
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author | Strasser, Richard |
author_facet | Strasser, Richard |
author_sort | Strasser, Richard |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-5045529 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-50455292016-10-03 Plant protein glycosylation Strasser, Richard Glycobiology Review 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. Oxford University Press 2016-09 2016-10-01 /pmc/articles/PMC5045529/ /pubmed/26911286 http://dx.doi.org/10.1093/glycob/cww023 Text en © The Author 2016. Published by Oxford University Press. http://creativecommons.org/licenses/by/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Review Strasser, Richard Plant protein glycosylation |
title | Plant protein glycosylation |
title_full | Plant protein glycosylation |
title_fullStr | Plant protein glycosylation |
title_full_unstemmed | Plant protein glycosylation |
title_short | Plant protein glycosylation |
title_sort | plant protein glycosylation |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5045529/ https://www.ncbi.nlm.nih.gov/pubmed/26911286 http://dx.doi.org/10.1093/glycob/cww023 |
work_keys_str_mv | AT strasserrichard plantproteinglycosylation |