Fasciclin-Like Arabinogalactan-Protein 16 (FLA16) Is Required for Stem Development in Arabidopsis
The predominant Fascilin 1 (FAS1)-containing proteins in plants belong to the Fasciclin-Like Arabinogalactan-protein (FLA) family of extracellular glycoproteins. In addition to FAS1 domains, these multi-domain FLA proteins contain glycomotif regions predicted to direct addition of large arabinogalac...
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Frontiers Media S.A.
2020-12-01
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Series: | Frontiers in Plant Science |
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Online Access: | https://www.frontiersin.org/articles/10.3389/fpls.2020.615392/full |
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author | Edgar Liu Colleen P. MacMillan Thomas Shafee Yingxuan Ma Yingxuan Ma Julian Ratcliffe Allison van de Meene Antony Bacic Antony Bacic John Humphries John Humphries Kim L. Johnson Kim L. Johnson |
author_facet | Edgar Liu Colleen P. MacMillan Thomas Shafee Yingxuan Ma Yingxuan Ma Julian Ratcliffe Allison van de Meene Antony Bacic Antony Bacic John Humphries John Humphries Kim L. Johnson Kim L. Johnson |
author_sort | Edgar Liu |
collection | DOAJ |
description | The predominant Fascilin 1 (FAS1)-containing proteins in plants belong to the Fasciclin-Like Arabinogalactan-protein (FLA) family of extracellular glycoproteins. In addition to FAS1 domains, these multi-domain FLA proteins contain glycomotif regions predicted to direct addition of large arabinogalactan (AG) glycans and many contain signal sequences for addition of a glycosylphosphatidylinositol (GPI)-anchor to tether them to the plasma membrane. FLAs are proposed to play both structural and signaling functions by forming a range of interactions in the plant extracellular matrix, similar to FAS1-containing proteins in animals. FLA group B members contain two FAS1 domains and are not predicted to be GPI-anchored. None of the group B members have been functionally characterized or their sub-cellular location resolved, limiting understanding of their function. We investigated the group B FLA16 in Arabidopsis that is predominantly expressed in inflorescence tissues. FLA16 is the most highly expressed FLA in the stem after Group A members FLA11 and FLA12 that are stem specific. A FLA16-YFP fusion protein driven by the endogenous putative FLA16 promoter in wild type background showed expression in cells with secondary cell walls, and FLA16 displayed characteristics of cell wall glycoproteins with moderate glycosylation. Investigation of a fla16 mutant showed loss of FLA16 leads to reduced stem length and altered biomechanical properties, likely as a result of reduced levels of cellulose. Immuno-labeling indicated support for FLA16 location to the plasma-membrane and (apoplastic) cell wall of interfascicular stem fiber cells. Together these results indicate FLA16, a two-FAS1 domain FLAs, plays a role in plant secondary cell wall synthesis and function. |
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spelling | doaj.art-3fe1fab519894c92bd8d25e8c4fbabaf2022-12-21T21:29:25ZengFrontiers Media S.A.Frontiers in Plant Science1664-462X2020-12-011110.3389/fpls.2020.615392615392Fasciclin-Like Arabinogalactan-Protein 16 (FLA16) Is Required for Stem Development in ArabidopsisEdgar Liu0Colleen P. MacMillan1Thomas Shafee2Yingxuan Ma3Yingxuan Ma4Julian Ratcliffe5Allison van de Meene6Antony Bacic7Antony Bacic8John Humphries9John Humphries10Kim L. Johnson11Kim L. Johnson12School of BioSciences, University of Melbourne, Parkville, VIC, AustraliaCSIRO, Agriculture and Food, CSIRO Black Mountain Science and Innovation Park, Canberra, ACT, AustraliaLa Trobe Institute for Agriculture and Food, Department of Animal, Plant and Soil Sciences, La Trobe University, Bundoora, VIC, AustraliaSchool of BioSciences, University of Melbourne, Parkville, VIC, AustraliaLa Trobe Institute for Agriculture and Food, Department of Animal, Plant and Soil Sciences, La Trobe University, Bundoora, VIC, AustraliaLa Trobe Institute for Agriculture and Food, Department of Animal, Plant and Soil Sciences, La Trobe University, Bundoora, VIC, AustraliaSchool of BioSciences, University of Melbourne, Parkville, VIC, AustraliaLa Trobe Institute for Agriculture and Food, Department of Animal, Plant and Soil Sciences, La Trobe University, Bundoora, VIC, AustraliaSino-Australia Plant Cell Wall Research Centre, College of Forestry and Biotechnology, Zhejiang A & F University, Hangzhou, ChinaSchool of BioSciences, University of Melbourne, Parkville, VIC, AustraliaLa Trobe Institute for Agriculture and Food, Department of Animal, Plant and Soil Sciences, La Trobe University, Bundoora, VIC, AustraliaLa Trobe Institute for Agriculture and Food, Department of Animal, Plant and Soil Sciences, La Trobe University, Bundoora, VIC, AustraliaSino-Australia Plant Cell Wall Research Centre, College of Forestry and Biotechnology, Zhejiang A & F University, Hangzhou, ChinaThe predominant Fascilin 1 (FAS1)-containing proteins in plants belong to the Fasciclin-Like Arabinogalactan-protein (FLA) family of extracellular glycoproteins. In addition to FAS1 domains, these multi-domain FLA proteins contain glycomotif regions predicted to direct addition of large arabinogalactan (AG) glycans and many contain signal sequences for addition of a glycosylphosphatidylinositol (GPI)-anchor to tether them to the plasma membrane. FLAs are proposed to play both structural and signaling functions by forming a range of interactions in the plant extracellular matrix, similar to FAS1-containing proteins in animals. FLA group B members contain two FAS1 domains and are not predicted to be GPI-anchored. None of the group B members have been functionally characterized or their sub-cellular location resolved, limiting understanding of their function. We investigated the group B FLA16 in Arabidopsis that is predominantly expressed in inflorescence tissues. FLA16 is the most highly expressed FLA in the stem after Group A members FLA11 and FLA12 that are stem specific. A FLA16-YFP fusion protein driven by the endogenous putative FLA16 promoter in wild type background showed expression in cells with secondary cell walls, and FLA16 displayed characteristics of cell wall glycoproteins with moderate glycosylation. Investigation of a fla16 mutant showed loss of FLA16 leads to reduced stem length and altered biomechanical properties, likely as a result of reduced levels of cellulose. Immuno-labeling indicated support for FLA16 location to the plasma-membrane and (apoplastic) cell wall of interfascicular stem fiber cells. Together these results indicate FLA16, a two-FAS1 domain FLAs, plays a role in plant secondary cell wall synthesis and function.https://www.frontiersin.org/articles/10.3389/fpls.2020.615392/fullcell wallglycoproteinfasciclin-like arabinogalactan-proteinstembiomechanics |
spellingShingle | Edgar Liu Colleen P. MacMillan Thomas Shafee Yingxuan Ma Yingxuan Ma Julian Ratcliffe Allison van de Meene Antony Bacic Antony Bacic John Humphries John Humphries Kim L. Johnson Kim L. Johnson Fasciclin-Like Arabinogalactan-Protein 16 (FLA16) Is Required for Stem Development in Arabidopsis Frontiers in Plant Science cell wall glycoprotein fasciclin-like arabinogalactan-protein stem biomechanics |
title | Fasciclin-Like Arabinogalactan-Protein 16 (FLA16) Is Required for Stem Development in Arabidopsis |
title_full | Fasciclin-Like Arabinogalactan-Protein 16 (FLA16) Is Required for Stem Development in Arabidopsis |
title_fullStr | Fasciclin-Like Arabinogalactan-Protein 16 (FLA16) Is Required for Stem Development in Arabidopsis |
title_full_unstemmed | Fasciclin-Like Arabinogalactan-Protein 16 (FLA16) Is Required for Stem Development in Arabidopsis |
title_short | Fasciclin-Like Arabinogalactan-Protein 16 (FLA16) Is Required for Stem Development in Arabidopsis |
title_sort | fasciclin like arabinogalactan protein 16 fla16 is required for stem development in arabidopsis |
topic | cell wall glycoprotein fasciclin-like arabinogalactan-protein stem biomechanics |
url | https://www.frontiersin.org/articles/10.3389/fpls.2020.615392/full |
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