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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Autores principales: Hijazi, M., Velasquez, S.M., Jamet, E., Estevez, J.M., Albenne, C.
Formato: JOUR
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Acceso en línea:http://hdl.handle.net/20.500.12110/paper_1664462X_v5_nAUG_p_Hijazi
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spelling 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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