Artículo

Xue, H.; Veit, C.; Abas, L.; Tryfona, T.; Maresch, D.; Ricardi, M.M.; Estevez, J.M.; Strasser, R.; Seifert, G.J. "Arabidopsis thaliana FLA4 functions as a glycan-stabilized soluble factor via its carboxy-proximal Fasciclin 1 domain" (2017) Plant Journal. 91(4):613-630
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Abstract:

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.

Registro:

Documento: Artículo
Título:Arabidopsis thaliana FLA4 functions as a glycan-stabilized soluble factor via its carboxy-proximal Fasciclin 1 domain
Autor:Xue, H.; Veit, C.; Abas, L.; Tryfona, T.; Maresch, D.; Ricardi, M.M.; Estevez, J.M.; Strasser, R.; Seifert, G.J.
Filiación:Department of Applied Genetics and Cell Biology, University of Natural Resources and Life Science, BOKU Vienna, Muthgasse 11, Vienna, A-1190, Austria
Department of Biochemistry, University of Cambridge, Cambridge, CB2 1QW, United Kingdom
Department of Chemistry, University of Natural Resources and Life Science, BOKU Vienna, Muthgasse 11, Vienna, A-1190, Austria
Biología Molecular y Neurociencias–Consejo Nacional de Investigaciones Científicas y Técnicas(IFIByNE-CONICET), Instituto de Fisiología, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Buenos Aires, C1428EGA, Argentina
Fundación Instituto Leloir and Instituto de Investigaciones Bioquímicas de Buenos Aires, Buenos Aires CP, C1405BWE, Argentina
Palabras clave: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
Año:2017
Volumen:91
Número:4
Página de inicio:613
Página de fin:630
DOI: http://dx.doi.org/10.1111/tpj.13591
Título revista:Plant Journal
Título revista abreviado:Plant J.
ISSN:09607412
CODEN:PLJUE
CAS:Arabidopsis Proteins; arabinogalactan proteins; Cell Adhesion Molecules; Glycoproteins; Luminescent Proteins; Mucoproteins; Plant Proteins; Polysaccharides; Recombinant Fusion Proteins; SOS5 protein, Arabidopsis
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_09607412_v91_n4_p613_Xue

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Citas:

---------- APA ----------
Xue, H., Veit, C., Abas, L., Tryfona, T., Maresch, D., Ricardi, M.M., Estevez, J.M.,..., Seifert, G.J. (2017) . Arabidopsis thaliana FLA4 functions as a glycan-stabilized soluble factor via its carboxy-proximal Fasciclin 1 domain. Plant Journal, 91(4), 613-630.
http://dx.doi.org/10.1111/tpj.13591
---------- CHICAGO ----------
Xue, H., Veit, C., Abas, L., Tryfona, T., Maresch, D., Ricardi, M.M., et al. "Arabidopsis thaliana FLA4 functions as a glycan-stabilized soluble factor via its carboxy-proximal Fasciclin 1 domain" . Plant Journal 91, no. 4 (2017) : 613-630.
http://dx.doi.org/10.1111/tpj.13591
---------- MLA ----------
Xue, H., Veit, C., Abas, L., Tryfona, T., Maresch, D., Ricardi, M.M., et al. "Arabidopsis thaliana FLA4 functions as a glycan-stabilized soluble factor via its carboxy-proximal Fasciclin 1 domain" . Plant Journal, vol. 91, no. 4, 2017, pp. 613-630.
http://dx.doi.org/10.1111/tpj.13591
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Xue, H., Veit, C., Abas, L., Tryfona, T., Maresch, D., Ricardi, M.M., et al. Arabidopsis thaliana FLA4 functions as a glycan-stabilized soluble factor via its carboxy-proximal Fasciclin 1 domain. Plant J. 2017;91(4):613-630.
http://dx.doi.org/10.1111/tpj.13591