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dc.contributor.author
Xue, Hui
dc.contributor.author
Veit, Christiane
dc.contributor.author
Abas, Lindy
dc.contributor.author
Tryfona, Theodora
dc.contributor.author
Maresch, Daniel
dc.contributor.author
Ricardi, Martiniano María
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dc.contributor.author
Estevez, Jose Manuel
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dc.contributor.author
Strasser, Richard
dc.contributor.author
Seifert, Georg J.
dc.date.available
2018-03-26T19:36:02Z
dc.date.issued
2017-08
dc.identifier.citation
Xue, Hui; Veit, Christiane; Abas, Lindy; Tryfona, Theodora; Maresch, Daniel; et al.; Arabidopsis thaliana FLA4 functions as a glycan-stabilized soluble factor via its carboxy-proximal Fasciclin 1 domain; Wiley Blackwell Publishing, Inc; Plant Journal; 91; 4; 8-2017; 613-630
dc.identifier.issn
0960-7412
dc.identifier.uri
http://hdl.handle.net/11336/39991
dc.description.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.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Wiley Blackwell Publishing, Inc
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dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Arabidopsis Thaliana
dc.subject
Arabinogalactan Protein
dc.subject
Fasciclin
dc.subject
Gpi-Anchor
dc.subject
N-Glycan
dc.subject
O-Glycan
dc.subject.classification
Otras Ciencias Biológicas
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dc.subject.classification
Ciencias Biológicas
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dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
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dc.title
Arabidopsis thaliana FLA4 functions as a glycan-stabilized soluble factor via its carboxy-proximal Fasciclin 1 domain
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2018-03-26T18:17:00Z
dc.journal.volume
91
dc.journal.number
4
dc.journal.pagination
613-630
dc.journal.pais
Reino Unido
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dc.journal.ciudad
Londres
dc.description.fil
Fil: Xue, Hui. University of Natural Resources and Life Science; Austria
dc.description.fil
Fil: Veit, Christiane. University of Natural Resources and Life Science; Austria
dc.description.fil
Fil: Abas, Lindy. University of Natural Resources and Life Science; Austria
dc.description.fil
Fil: Tryfona, Theodora. University of Cambridge; Reino Unido
dc.description.fil
Fil: Maresch, Daniel. University of Natural Resources and Life Science; Austria
dc.description.fil
Fil: Ricardi, Martiniano María. 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: 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. Fundación Instituto Leloir; Argentina
dc.description.fil
Fil: Strasser, Richard. University of Natural Resources and Life Science; Austria
dc.description.fil
Fil: Seifert, Georg J.. University of Natural Resources and Life Science; Austria
dc.journal.title
Plant Journal
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dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://onlinelibrary.wiley.com/doi/10.1111/tpj.13591
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1111/tpj.13591
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