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dc.contributor.author
Hijazi, May  
dc.contributor.author
Velásquez, Silvia Melina  
dc.contributor.author
Jamet, Elisabeth  
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Estevez, Jose Manuel  
dc.contributor.author
Albenne, Cécile  
dc.date.available
2017-07-17T20:37:26Z  
dc.date.issued
2014-08  
dc.identifier.citation
Hijazi, May; Velásquez, Silvia Melina; Jamet, Elisabeth; Estevez, Jose Manuel; Albenne, Cécile; An update on post-translational modifications of hydroxyproline-rich glycoproteins: toward a model highlighting their contribution to plant cell wall architecture; Frontiers; Frontiers in Plant Science; 5; 8-2014; 1-10; 395  
dc.identifier.uri
http://hdl.handle.net/11336/20746  
dc.description.abstract
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-, weakly- or 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.  
dc.format
application/pdf  
dc.language.iso
eng  
dc.publisher
Frontiers  
dc.rights
info:eu-repo/semantics/openAccess  
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/  
dc.subject
O-Glycosylation  
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Arabinogalactan Protein  
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Extensin  
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Hydroxyproline  
dc.subject.classification
Bioquímica y Biología Molecular  
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Ciencias Biológicas  
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CIENCIAS NATURALES Y EXACTAS  
dc.title
An update on post-translational modifications of hydroxyproline-rich glycoproteins: toward a model highlighting their contribution to plant cell wall architecture  
dc.type
info:eu-repo/semantics/article  
dc.type
info:ar-repo/semantics/artículo  
dc.type
info:eu-repo/semantics/publishedVersion  
dc.date.updated
2017-07-11T19:27:28Z  
dc.identifier.eissn
1664-462X  
dc.journal.volume
5  
dc.journal.pagination
1-10; 395  
dc.journal.pais
Suiza  
dc.description.fil
Fil: Hijazi, May. Centre National de la Recherche Scientifique; Francia. Université de Toulouse; Francia  
dc.description.fil
Fil: Velásquez, Silvia Melina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Fisiología, Biología Molecular y Neurociencias. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Fisiología, Biología Molecular y Neurociencias; Argentina  
dc.description.fil
Fil: Jamet, Elisabeth. Centre National de la Recherche Scientifique; Francia. Université de Toulouse; Francia  
dc.description.fil
Fil: Estevez, Jose Manuel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Fisiología, Biología Molecular y Neurociencias. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Fisiología, Biología Molecular y Neurociencias; Argentina  
dc.description.fil
Fil: Albenne, Cécile. Centre National de la Recherche Scientifique; Francia. Université de Toulouse; Francia  
dc.journal.title
Frontiers in Plant Science  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.3389/fpls.2014.00395  
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info:eu-repo/semantics/altIdentifier/url/http://journal.frontiersin.org/article/10.3389/fpls.2014.00395/full