An update on post-translational modifications of hydroxyproline-rich glycoproteins: Toward a model highlighting their contribution to plant cell wall architecture
Plant cell walls are composite structures mainly composed of polysaccharides, also containing a large set of proteins involved in diverse functions such as growth, environmental sensing, signaling, and defense. Research on cell wall proteins (CWPs) is a challenging field since present knowledge of t...
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todo:paper_1664462X_v5_nAUG_p_Hijazi2023-10-03T16:29:11Z An update on post-translational modifications of hydroxyproline-rich glycoproteins: Toward a model highlighting their contribution to plant cell wall architecture Hijazi, M. Velasquez, S.M. Jamet, E. Estevez, J.M. Albenne, C. Arabinogalactan protein Extensin Hydroxyproline O-glycosylation Proline-rich protein Plant cell walls are composite structures mainly composed of polysaccharides, also containing a large set of proteins involved in diverse functions such as growth, environmental sensing, signaling, and defense. Research on cell wall proteins (CWPs) is a challenging field since present knowledge of their role into the structure and function of cell walls is very incomplete. Among CWPs, hydroxyproline (Hyp)-rich O-glycoproteins (HRGPs) were classified into three categories: (i) moderately glycosylated extensins (EXTs) able to form covalent scaffolds; (ii) hyperglycosylated arabinogalactan proteins (AGPs); and (iii) Hyp/proline (Pro)-Rich proteins (H/PRPs) that may be non-, weaklyor highly-glycosylated. In this review, we provide a description of the main features of their post-translational modifications (PTMs), biosynthesis, structure, and function. We propose a new model integrating HRGPs and their partners in cell walls. Altogether, they could form a continuous glyco-network with non-cellulosic polysaccharides via covalent bonds or non-covalent interactions, thus strongly contributing to cell wall architecture. © 2014 Hijazi, Velasquez, Jamet, Estevez and Albenne. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_1664462X_v5_nAUG_p_Hijazi |
institution |
Universidad de Buenos Aires |
institution_str |
I-28 |
repository_str |
R-134 |
collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
topic |
Arabinogalactan protein Extensin Hydroxyproline O-glycosylation Proline-rich protein |
spellingShingle |
Arabinogalactan protein Extensin Hydroxyproline O-glycosylation Proline-rich protein Hijazi, M. Velasquez, S.M. Jamet, E. Estevez, J.M. Albenne, C. An update on post-translational modifications of hydroxyproline-rich glycoproteins: Toward a model highlighting their contribution to plant cell wall architecture |
topic_facet |
Arabinogalactan protein Extensin Hydroxyproline O-glycosylation Proline-rich protein |
description |
Plant cell walls are composite structures mainly composed of polysaccharides, also containing a large set of proteins involved in diverse functions such as growth, environmental sensing, signaling, and defense. Research on cell wall proteins (CWPs) is a challenging field since present knowledge of their role into the structure and function of cell walls is very incomplete. Among CWPs, hydroxyproline (Hyp)-rich O-glycoproteins (HRGPs) were classified into three categories: (i) moderately glycosylated extensins (EXTs) able to form covalent scaffolds; (ii) hyperglycosylated arabinogalactan proteins (AGPs); and (iii) Hyp/proline (Pro)-Rich proteins (H/PRPs) that may be non-, weaklyor highly-glycosylated. In this review, we provide a description of the main features of their post-translational modifications (PTMs), biosynthesis, structure, and function. We propose a new model integrating HRGPs and their partners in cell walls. Altogether, they could form a continuous glyco-network with non-cellulosic polysaccharides via covalent bonds or non-covalent interactions, thus strongly contributing to cell wall architecture. © 2014 Hijazi, Velasquez, Jamet, Estevez and Albenne. |
format |
JOUR |
author |
Hijazi, M. Velasquez, S.M. Jamet, E. Estevez, J.M. Albenne, C. |
author_facet |
Hijazi, M. Velasquez, S.M. Jamet, E. Estevez, J.M. Albenne, C. |
author_sort |
Hijazi, M. |
title |
An update on post-translational modifications of hydroxyproline-rich glycoproteins: Toward a model highlighting their contribution to plant cell wall architecture |
title_short |
An update on post-translational modifications of hydroxyproline-rich glycoproteins: Toward a model highlighting their contribution to plant cell wall architecture |
title_full |
An update on post-translational modifications of hydroxyproline-rich glycoproteins: Toward a model highlighting their contribution to plant cell wall architecture |
title_fullStr |
An update on post-translational modifications of hydroxyproline-rich glycoproteins: Toward a model highlighting their contribution to plant cell wall architecture |
title_full_unstemmed |
An update on post-translational modifications of hydroxyproline-rich glycoproteins: Toward a model highlighting their contribution to plant cell wall architecture |
title_sort |
update on post-translational modifications of hydroxyproline-rich glycoproteins: toward a model highlighting their contribution to plant cell wall architecture |
url |
http://hdl.handle.net/20.500.12110/paper_1664462X_v5_nAUG_p_Hijazi |
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