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Directed growth and fusion of membrane-wall microdomains requires CASP-mediated inhibition and displacement of secretory foci
Casparian strips (CS) are aligned bands of lignin-impregnated cell walls, building an extracellular diffusion barrier in roots. Their structure profoundly differs from tight junctions (TJ), analogous structures in animals. Nonetheless, CS membrane domain (CSD) proteins 1-5 (CASP1-5) are homologues o...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Nature Publishing Group UK
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10036488/ https://www.ncbi.nlm.nih.gov/pubmed/36959183 http://dx.doi.org/10.1038/s41467-023-37265-7 |
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author | Barbosa, Inês Catarina Ramos De Bellis, Damien Flückiger, Isabelle Bellani, Etienne Grangé-Guerment, Mathieu Hématy, Kian Geldner, Niko |
author_facet | Barbosa, Inês Catarina Ramos De Bellis, Damien Flückiger, Isabelle Bellani, Etienne Grangé-Guerment, Mathieu Hématy, Kian Geldner, Niko |
author_sort | Barbosa, Inês Catarina Ramos |
collection | PubMed |
description | Casparian strips (CS) are aligned bands of lignin-impregnated cell walls, building an extracellular diffusion barrier in roots. Their structure profoundly differs from tight junctions (TJ), analogous structures in animals. Nonetheless, CS membrane domain (CSD) proteins 1-5 (CASP1-5) are homologues of occludins, TJ components. CASP-marked membranes display cell wall (matrix) adhesion and membrane protein exclusion. A full CASP knock-out now reveals CASPs are not needed for localized lignification, since correctly positioned lignin microdomains still form in the mutant. Ultra-structurally, however, these microdomains are disorganized, showing excessive cell wall growth, lack of exclusion zone and matrix adhesion, and impaired exocyst dynamics. Proximity-labelling identifies a Rab-GTPase subfamily, known exocyst activators, as potential CASP-interactors and demonstrate their localization and function at the CSD. We propose that CASP microdomains displace initial secretory foci by excluding vesicle tethering factors, thereby ensuring rapid fusion of microdomains into a membrane-cell wall band that seals the extracellular space. |
format | Online Article Text |
id | pubmed-10036488 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-100364882023-03-25 Directed growth and fusion of membrane-wall microdomains requires CASP-mediated inhibition and displacement of secretory foci Barbosa, Inês Catarina Ramos De Bellis, Damien Flückiger, Isabelle Bellani, Etienne Grangé-Guerment, Mathieu Hématy, Kian Geldner, Niko Nat Commun Article Casparian strips (CS) are aligned bands of lignin-impregnated cell walls, building an extracellular diffusion barrier in roots. Their structure profoundly differs from tight junctions (TJ), analogous structures in animals. Nonetheless, CS membrane domain (CSD) proteins 1-5 (CASP1-5) are homologues of occludins, TJ components. CASP-marked membranes display cell wall (matrix) adhesion and membrane protein exclusion. A full CASP knock-out now reveals CASPs are not needed for localized lignification, since correctly positioned lignin microdomains still form in the mutant. Ultra-structurally, however, these microdomains are disorganized, showing excessive cell wall growth, lack of exclusion zone and matrix adhesion, and impaired exocyst dynamics. Proximity-labelling identifies a Rab-GTPase subfamily, known exocyst activators, as potential CASP-interactors and demonstrate their localization and function at the CSD. We propose that CASP microdomains displace initial secretory foci by excluding vesicle tethering factors, thereby ensuring rapid fusion of microdomains into a membrane-cell wall band that seals the extracellular space. Nature Publishing Group UK 2023-03-23 /pmc/articles/PMC10036488/ /pubmed/36959183 http://dx.doi.org/10.1038/s41467-023-37265-7 Text en © The Author(s) 2023 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Article Barbosa, Inês Catarina Ramos De Bellis, Damien Flückiger, Isabelle Bellani, Etienne Grangé-Guerment, Mathieu Hématy, Kian Geldner, Niko Directed growth and fusion of membrane-wall microdomains requires CASP-mediated inhibition and displacement of secretory foci |
title | Directed growth and fusion of membrane-wall microdomains requires CASP-mediated inhibition and displacement of secretory foci |
title_full | Directed growth and fusion of membrane-wall microdomains requires CASP-mediated inhibition and displacement of secretory foci |
title_fullStr | Directed growth and fusion of membrane-wall microdomains requires CASP-mediated inhibition and displacement of secretory foci |
title_full_unstemmed | Directed growth and fusion of membrane-wall microdomains requires CASP-mediated inhibition and displacement of secretory foci |
title_short | Directed growth and fusion of membrane-wall microdomains requires CASP-mediated inhibition and displacement of secretory foci |
title_sort | directed growth and fusion of membrane-wall microdomains requires casp-mediated inhibition and displacement of secretory foci |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10036488/ https://www.ncbi.nlm.nih.gov/pubmed/36959183 http://dx.doi.org/10.1038/s41467-023-37265-7 |
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