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Recent Developments in Deciphering the Biological Role of Plant Complex N-Glycans

Asparagine (N)-linked protein glycosylation is a ubiquitous co- and posttranslational modification which has a huge impact on the biogenesis and function of proteins and consequently on the development, growth, and physiology of organisms. In mammals, N-glycan processing carried out by Golgi-residen...

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Autor principal: Strasser, Richard
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9085483/
https://www.ncbi.nlm.nih.gov/pubmed/35557740
http://dx.doi.org/10.3389/fpls.2022.897549
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author Strasser, Richard
author_facet Strasser, Richard
author_sort Strasser, Richard
collection PubMed
description Asparagine (N)-linked protein glycosylation is a ubiquitous co- and posttranslational modification which has a huge impact on the biogenesis and function of proteins and consequently on the development, growth, and physiology of organisms. In mammals, N-glycan processing carried out by Golgi-resident glycosidases and glycosyltransferases creates a number of structurally diverse N-glycans with specific roles in many different biological processes. In plants, complex N-glycan modifications like the attachment of β1,2-xylose, core α1,3-fucose, or the Lewis A-type structures are evolutionary highly conserved, but their biological function is poorly known. Here, I highlight recent developments that contribute to a better understanding of these conserved glycoprotein modifications and discuss future directions to move the field forward.
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spelling pubmed-90854832022-05-11 Recent Developments in Deciphering the Biological Role of Plant Complex N-Glycans Strasser, Richard Front Plant Sci Plant Science Asparagine (N)-linked protein glycosylation is a ubiquitous co- and posttranslational modification which has a huge impact on the biogenesis and function of proteins and consequently on the development, growth, and physiology of organisms. In mammals, N-glycan processing carried out by Golgi-resident glycosidases and glycosyltransferases creates a number of structurally diverse N-glycans with specific roles in many different biological processes. In plants, complex N-glycan modifications like the attachment of β1,2-xylose, core α1,3-fucose, or the Lewis A-type structures are evolutionary highly conserved, but their biological function is poorly known. Here, I highlight recent developments that contribute to a better understanding of these conserved glycoprotein modifications and discuss future directions to move the field forward. Frontiers Media S.A. 2022-04-25 /pmc/articles/PMC9085483/ /pubmed/35557740 http://dx.doi.org/10.3389/fpls.2022.897549 Text en Copyright © 2022 Strasser. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Plant Science
Strasser, Richard
Recent Developments in Deciphering the Biological Role of Plant Complex N-Glycans
title Recent Developments in Deciphering the Biological Role of Plant Complex N-Glycans
title_full Recent Developments in Deciphering the Biological Role of Plant Complex N-Glycans
title_fullStr Recent Developments in Deciphering the Biological Role of Plant Complex N-Glycans
title_full_unstemmed Recent Developments in Deciphering the Biological Role of Plant Complex N-Glycans
title_short Recent Developments in Deciphering the Biological Role of Plant Complex N-Glycans
title_sort recent developments in deciphering the biological role of plant complex n-glycans
topic Plant Science
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9085483/
https://www.ncbi.nlm.nih.gov/pubmed/35557740
http://dx.doi.org/10.3389/fpls.2022.897549
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