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

Hui Xue, Christiane Veit, Lindy Abas, Theodora Tryfona, Daniel Maresch, Martiniano M. Ricardi, José Manuel Estevez, Richard Strasser, Georg J. Seifert

Resultado de la investigación: Article

7 Citas (Scopus)

Resumen

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.

Idioma originalEnglish
Páginas (desde-hasta)613-630
Número de páginas18
PublicaciónPlant Journal
Volumen91
N.º4
DOI
EstadoPublished - ago 2017

Huella dactilar

glycosylation
Glycosylation
Arabidopsis
Polysaccharides
polysaccharides
Arabidopsis thaliana
arabinogalactan proteins
plasma membrane
Cell Membrane
Endoplasmic Reticulum
endoplasmic reticulum
endosomes
Endosomes
apoplast
epitopes
glycoproteins
Epitopes
Glycoproteins
Proteins
proteins

ASJC Scopus subject areas

  • Genetics
  • Plant Science
  • Cell Biology

Citar esto

Xue, H., Veit, C., Abas, L., Tryfona, T., Maresch, D., Ricardi, M. 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. https://doi.org/10.1111/tpj.13591
Xue, Hui ; Veit, Christiane ; Abas, Lindy ; Tryfona, Theodora ; Maresch, Daniel ; Ricardi, Martiniano M. ; Estevez, José Manuel ; Strasser, Richard ; Seifert, Georg J. / Arabidopsis thaliana FLA4 functions as a glycan-stabilized soluble factor via its carboxy-proximal Fasciclin 1 domain. En: Plant Journal. 2017 ; Vol. 91, N.º 4. pp. 613-630.
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title = "Arabidopsis thaliana FLA4 functions as a glycan-stabilized soluble factor via its carboxy-proximal Fasciclin 1 domain",
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.",
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Xue, H, Veit, C, Abas, L, Tryfona, T, Maresch, D, Ricardi, MM, Estevez, JM, Strasser, R & Seifert, GJ 2017, 'Arabidopsis thaliana FLA4 functions as a glycan-stabilized soluble factor via its carboxy-proximal Fasciclin 1 domain', Plant Journal, vol. 91, n.º 4, pp. 613-630. https://doi.org/10.1111/tpj.13591

Arabidopsis thaliana FLA4 functions as a glycan-stabilized soluble factor via its carboxy-proximal Fasciclin 1 domain. / Xue, Hui; Veit, Christiane; Abas, Lindy; Tryfona, Theodora; Maresch, Daniel; Ricardi, Martiniano M.; Estevez, José Manuel; Strasser, Richard; Seifert, Georg J.

En: Plant Journal, Vol. 91, N.º 4, 08.2017, p. 613-630.

Resultado de la investigación: Article

TY - JOUR

T1 - Arabidopsis thaliana FLA4 functions as a glycan-stabilized soluble factor via its carboxy-proximal Fasciclin 1 domain

AU - Xue, Hui

AU - Veit, Christiane

AU - Abas, Lindy

AU - Tryfona, Theodora

AU - Maresch, Daniel

AU - Ricardi, Martiniano M.

AU - Estevez, José Manuel

AU - Strasser, Richard

AU - Seifert, Georg J.

PY - 2017/8

Y1 - 2017/8

N2 - 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.

AB - 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.

KW - Arabidopsis thaliana

KW - arabinogalactan protein

KW - fasciclin

KW - GPI-anchor

KW - N-glycan

KW - O-glycan

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U2 - 10.1111/tpj.13591

DO - 10.1111/tpj.13591

M3 - Article

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EP - 630

JO - Plant Journal

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