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Analysis of exocyst function in endodermis reveals its widespread contribution and specificity of action

The exocyst is the main plasma membrane vesicle-tethering complex in eukaryotes and is composed of eight different subunits. Yet, in plant genomes, many subunits display multiple copies, thought to reflect evolution of complex subtypes with divergent functions. In Arabidopsis thaliana root endoderma...

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Autores principales: Hématy, Kian, De Bellis, Damien, Wang, Xin, Mähönen, Ari Pekka, Geldner, Niko
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9157074/
https://www.ncbi.nlm.nih.gov/pubmed/35099565
http://dx.doi.org/10.1093/plphys/kiac019
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author Hématy, Kian
De Bellis, Damien
Wang, Xin
Mähönen, Ari Pekka
Geldner, Niko
author_facet Hématy, Kian
De Bellis, Damien
Wang, Xin
Mähönen, Ari Pekka
Geldner, Niko
author_sort Hématy, Kian
collection PubMed
description The exocyst is the main plasma membrane vesicle-tethering complex in eukaryotes and is composed of eight different subunits. Yet, in plant genomes, many subunits display multiple copies, thought to reflect evolution of complex subtypes with divergent functions. In Arabidopsis thaliana root endodermal cells, the isoform EXO70A1 is required for positioning of CASP1 at the Casparian Strip Domain, but not for its non-targeted secretion to the plasma membrane. Here, we show that exo84b resembles exo70a1 mutants regarding CASP1 mistargeting and secretion of apoplastic proteins, but exo84b additionally affects secretion of other integral plasma membrane proteins. Moreover, conditional, cell-type-specific gene editing of the single-copy core component SEC6 allows visualization of secretion defects in plant cells with a complete lack of exocyst complex function. Our approach opens avenues for deciphering the complexity/diversity of exocyst functions in plant cells and enables analysis of central trafficking components with lethal phenotypes.
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spelling pubmed-91570742022-06-04 Analysis of exocyst function in endodermis reveals its widespread contribution and specificity of action Hématy, Kian De Bellis, Damien Wang, Xin Mähönen, Ari Pekka Geldner, Niko Plant Physiol Research Articles The exocyst is the main plasma membrane vesicle-tethering complex in eukaryotes and is composed of eight different subunits. Yet, in plant genomes, many subunits display multiple copies, thought to reflect evolution of complex subtypes with divergent functions. In Arabidopsis thaliana root endodermal cells, the isoform EXO70A1 is required for positioning of CASP1 at the Casparian Strip Domain, but not for its non-targeted secretion to the plasma membrane. Here, we show that exo84b resembles exo70a1 mutants regarding CASP1 mistargeting and secretion of apoplastic proteins, but exo84b additionally affects secretion of other integral plasma membrane proteins. Moreover, conditional, cell-type-specific gene editing of the single-copy core component SEC6 allows visualization of secretion defects in plant cells with a complete lack of exocyst complex function. Our approach opens avenues for deciphering the complexity/diversity of exocyst functions in plant cells and enables analysis of central trafficking components with lethal phenotypes. Oxford University Press 2022-01-31 /pmc/articles/PMC9157074/ /pubmed/35099565 http://dx.doi.org/10.1093/plphys/kiac019 Text en © The Author(s) 2022. Published by Oxford University Press on behalf of American Society of Plant Biologists. https://creativecommons.org/licenses/by-nc-nd/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivs licence (https://creativecommons.org/licenses/by-nc-nd/4.0/), which permits non-commercial reproduction and distribution of the work, in any medium, provided the original work is not altered or transformed in any way, and that the work is properly cited. For commercial re-use, please contact journals.permissions@oup.com
spellingShingle Research Articles
Hématy, Kian
De Bellis, Damien
Wang, Xin
Mähönen, Ari Pekka
Geldner, Niko
Analysis of exocyst function in endodermis reveals its widespread contribution and specificity of action
title Analysis of exocyst function in endodermis reveals its widespread contribution and specificity of action
title_full Analysis of exocyst function in endodermis reveals its widespread contribution and specificity of action
title_fullStr Analysis of exocyst function in endodermis reveals its widespread contribution and specificity of action
title_full_unstemmed Analysis of exocyst function in endodermis reveals its widespread contribution and specificity of action
title_short Analysis of exocyst function in endodermis reveals its widespread contribution and specificity of action
title_sort analysis of exocyst function in endodermis reveals its widespread contribution and specificity of action
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9157074/
https://www.ncbi.nlm.nih.gov/pubmed/35099565
http://dx.doi.org/10.1093/plphys/kiac019
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