Arabidopsis thaliana FLA4 functions as a glycan-stabilized soluble factor via its carboxy-proximal Fasciclin 1 domain

Fasciclin-like arabinogalactan proteins (FLAs) are involved in numerous important functions in plants but the relevance of their complex structure to physiological function and cellular fate is unresolved. Using a fully functional fluorescent version of Arabidopsis thaliana FLA4 we show that this pr...

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Autores principales:	Ricardi, Martiniano Maria, Estevez, Jose Manuel
Publicado:	2017
Materias:	Arabidopsis thaliana arabinogalactan protein fasciclin GPI-anchor N-glycan O-glycan Cell membranes Glycosylation Proteins Arabinogalactan proteins Fasciclin GPI anchors Polysaccharides Plants Arabidopsis protein arabinogalactan proteins cell adhesion molecule glycoprotein hybrid protein mucoprotein photoprotein plant protein polysaccharide SOS5 protein, Arabidopsis Arabidopsis cytology endoplasmic reticulum genetics glycosylation metabolism plant root protein domain protein transport Arabidopsis Proteins Cell Adhesion Molecules Endoplasmic Reticulum Glycoproteins Luminescent Proteins Mucoproteins Plant Proteins Plant Roots Protein Domains Protein Transport Recombinant Fusion Proteins
Acceso en línea:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_09607412_v91_n4_p613_Xue http://hdl.handle.net/20.500.12110/paper_09607412_v91_n4_p613_Xue
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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spelling	paper:paper_09607412_v91_n4_p613_Xue2023-06-08T15:57:43Z Arabidopsis thaliana FLA4 functions as a glycan-stabilized soluble factor via its carboxy-proximal Fasciclin 1 domain Ricardi, Martiniano Maria Estevez, Jose Manuel Arabidopsis thaliana arabinogalactan protein fasciclin GPI-anchor N-glycan O-glycan Cell membranes Glycosylation Proteins Arabidopsis thaliana Arabinogalactan proteins Fasciclin GPI anchors N-glycan Polysaccharides Plants Proteins Arabidopsis protein arabinogalactan proteins cell adhesion molecule glycoprotein hybrid protein mucoprotein photoprotein plant protein polysaccharide SOS5 protein, Arabidopsis Arabidopsis cytology endoplasmic reticulum genetics glycosylation metabolism plant root protein domain protein transport Arabidopsis Arabidopsis Proteins Cell Adhesion Molecules Endoplasmic Reticulum Glycoproteins Glycosylation Luminescent Proteins Mucoproteins Plant Proteins Plant Roots Polysaccharides Protein Domains Protein Transport Recombinant Fusion Proteins Fasciclin-like arabinogalactan proteins (FLAs) are involved in numerous important functions in plants but the relevance of their complex structure to physiological function and cellular fate is unresolved. Using a fully functional fluorescent version of Arabidopsis thaliana FLA4 we show that this protein is localized at the plasma membrane as well as in endosomes and soluble in the apoplast. FLA4 is likely to be GPI-anchored, is highly N-glycosylated and carries two O-glycan epitopes previously associated with arabinogalactan proteins. The activity of FLA4 was resistant against deletion of the amino-proximal fasciclin 1 domain and was unaffected by removal of the GPI-modification signal, a highly conserved N-glycan or the deletion of predicted O-glycosylation sites. Nonetheless these structural changes dramatically decreased endoplasmic reticulum (ER)-exit and plasma membrane localization of FLA4, with N-glycosylation acting at the level of ER-exit and O-glycosylation influencing post-secretory fate. We show that FLA4 acts predominantly by molecular interactions involving its carboxy-proximal fasciclin 1 domain and that its amino-proximal fasciclin 1 domain is required for stabilization of plasma membrane localization. FLA4 functions as a soluble glycoprotein via its carboxy-proximal Fas1 domain and its normal cellular trafficking depends on N- and O-glycosylation. © 2017 The Authors. The Plant Journal published by John Wiley & Sons Ltd and Society for Experimental Biology. Fil:Ricardi, M.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Estevez, J.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2017 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_09607412_v91_n4_p613_Xue http://hdl.handle.net/20.500.12110/paper_09607412_v91_n4_p613_Xue
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	Arabidopsis thaliana arabinogalactan protein fasciclin GPI-anchor N-glycan O-glycan Cell membranes Glycosylation Proteins Arabidopsis thaliana Arabinogalactan proteins Fasciclin GPI anchors N-glycan Polysaccharides Plants Proteins Arabidopsis protein arabinogalactan proteins cell adhesion molecule glycoprotein hybrid protein mucoprotein photoprotein plant protein polysaccharide SOS5 protein, Arabidopsis Arabidopsis cytology endoplasmic reticulum genetics glycosylation metabolism plant root protein domain protein transport Arabidopsis Arabidopsis Proteins Cell Adhesion Molecules Endoplasmic Reticulum Glycoproteins Glycosylation Luminescent Proteins Mucoproteins Plant Proteins Plant Roots Polysaccharides Protein Domains Protein Transport Recombinant Fusion Proteins
spellingShingle	Arabidopsis thaliana arabinogalactan protein fasciclin GPI-anchor N-glycan O-glycan Cell membranes Glycosylation Proteins Arabidopsis thaliana Arabinogalactan proteins Fasciclin GPI anchors N-glycan Polysaccharides Plants Proteins Arabidopsis protein arabinogalactan proteins cell adhesion molecule glycoprotein hybrid protein mucoprotein photoprotein plant protein polysaccharide SOS5 protein, Arabidopsis Arabidopsis cytology endoplasmic reticulum genetics glycosylation metabolism plant root protein domain protein transport Arabidopsis Arabidopsis Proteins Cell Adhesion Molecules Endoplasmic Reticulum Glycoproteins Glycosylation Luminescent Proteins Mucoproteins Plant Proteins Plant Roots Polysaccharides Protein Domains Protein Transport Recombinant Fusion Proteins Ricardi, Martiniano Maria Estevez, Jose Manuel Arabidopsis thaliana FLA4 functions as a glycan-stabilized soluble factor via its carboxy-proximal Fasciclin 1 domain
topic_facet	Arabidopsis thaliana arabinogalactan protein fasciclin GPI-anchor N-glycan O-glycan Cell membranes Glycosylation Proteins Arabidopsis thaliana Arabinogalactan proteins Fasciclin GPI anchors N-glycan Polysaccharides Plants Proteins Arabidopsis protein arabinogalactan proteins cell adhesion molecule glycoprotein hybrid protein mucoprotein photoprotein plant protein polysaccharide SOS5 protein, Arabidopsis Arabidopsis cytology endoplasmic reticulum genetics glycosylation metabolism plant root protein domain protein transport Arabidopsis Arabidopsis Proteins Cell Adhesion Molecules Endoplasmic Reticulum Glycoproteins Glycosylation Luminescent Proteins Mucoproteins Plant Proteins Plant Roots Polysaccharides Protein Domains Protein Transport Recombinant Fusion Proteins
description	Fasciclin-like arabinogalactan proteins (FLAs) are involved in numerous important functions in plants but the relevance of their complex structure to physiological function and cellular fate is unresolved. Using a fully functional fluorescent version of Arabidopsis thaliana FLA4 we show that this protein is localized at the plasma membrane as well as in endosomes and soluble in the apoplast. FLA4 is likely to be GPI-anchored, is highly N-glycosylated and carries two O-glycan epitopes previously associated with arabinogalactan proteins. The activity of FLA4 was resistant against deletion of the amino-proximal fasciclin 1 domain and was unaffected by removal of the GPI-modification signal, a highly conserved N-glycan or the deletion of predicted O-glycosylation sites. Nonetheless these structural changes dramatically decreased endoplasmic reticulum (ER)-exit and plasma membrane localization of FLA4, with N-glycosylation acting at the level of ER-exit and O-glycosylation influencing post-secretory fate. We show that FLA4 acts predominantly by molecular interactions involving its carboxy-proximal fasciclin 1 domain and that its amino-proximal fasciclin 1 domain is required for stabilization of plasma membrane localization. FLA4 functions as a soluble glycoprotein via its carboxy-proximal Fas1 domain and its normal cellular trafficking depends on N- and O-glycosylation. © 2017 The Authors. The Plant Journal published by John Wiley & Sons Ltd and Society for Experimental Biology.
author	Ricardi, Martiniano Maria Estevez, Jose Manuel
author_facet	Ricardi, Martiniano Maria Estevez, Jose Manuel
author_sort	Ricardi, Martiniano Maria
title	Arabidopsis thaliana FLA4 functions as a glycan-stabilized soluble factor via its carboxy-proximal Fasciclin 1 domain
title_short	Arabidopsis thaliana FLA4 functions as a glycan-stabilized soluble factor via its carboxy-proximal Fasciclin 1 domain
title_full	Arabidopsis thaliana FLA4 functions as a glycan-stabilized soluble factor via its carboxy-proximal Fasciclin 1 domain
title_fullStr	Arabidopsis thaliana FLA4 functions as a glycan-stabilized soluble factor via its carboxy-proximal Fasciclin 1 domain
title_full_unstemmed	Arabidopsis thaliana FLA4 functions as a glycan-stabilized soluble factor via its carboxy-proximal Fasciclin 1 domain
title_sort	arabidopsis thaliana fla4 functions as a glycan-stabilized soluble factor via its carboxy-proximal fasciclin 1 domain
publishDate	2017
url	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_09607412_v91_n4_p613_Xue http://hdl.handle.net/20.500.12110/paper_09607412_v91_n4_p613_Xue
work_keys_str_mv	AT ricardimartinianomaria arabidopsisthalianafla4functionsasaglycanstabilizedsolublefactorviaitscarboxyproximalfasciclin1domain AT estevezjosemanuel arabidopsisthalianafla4functionsasaglycanstabilizedsolublefactorviaitscarboxyproximalfasciclin1domain
_version_	1768545886945673216

Arabidopsis thaliana FLA4 functions as a glycan-stabilized soluble factor via its carboxy-proximal Fasciclin 1 domain

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