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Stabilization of membrane topologies by proteinaceous remorin scaffolds
In plants, the topological organization of membranes has mainly been attributed to the cell wall and the cytoskeleton. Additionally, few proteins, such as plant-specific remorins have been shown to function as protein and lipid organizers. Root nodule symbiosis requires continuous membrane re-arrang...
Autores principales: | , , , , , , , , , , , , , , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9852587/ https://www.ncbi.nlm.nih.gov/pubmed/36658193 http://dx.doi.org/10.1038/s41467-023-35976-5 |
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author | Su, Chao Rodriguez-Franco, Marta Lace, Beatrice Nebel, Nils Hernandez-Reyes, Casandra Liang, Pengbo Schulze, Eija Mymrikov, Evgeny V. Gross, Nikolas M. Knerr, Julian Wang, Hong Siukstaite, Lina Keller, Jean Libourel, Cyril Fischer, Alexandra A. M. Gabor, Katharina E. Mark, Eric Popp, Claudia Hunte, Carola Weber, Wilfried Wendler, Petra Stanislas, Thomas Delaux, Pierre-Marc Einsle, Oliver Grosse, Robert Römer, Winfried Ott, Thomas |
author_facet | Su, Chao Rodriguez-Franco, Marta Lace, Beatrice Nebel, Nils Hernandez-Reyes, Casandra Liang, Pengbo Schulze, Eija Mymrikov, Evgeny V. Gross, Nikolas M. Knerr, Julian Wang, Hong Siukstaite, Lina Keller, Jean Libourel, Cyril Fischer, Alexandra A. M. Gabor, Katharina E. Mark, Eric Popp, Claudia Hunte, Carola Weber, Wilfried Wendler, Petra Stanislas, Thomas Delaux, Pierre-Marc Einsle, Oliver Grosse, Robert Römer, Winfried Ott, Thomas |
author_sort | Su, Chao |
collection | PubMed |
description | In plants, the topological organization of membranes has mainly been attributed to the cell wall and the cytoskeleton. Additionally, few proteins, such as plant-specific remorins have been shown to function as protein and lipid organizers. Root nodule symbiosis requires continuous membrane re-arrangements, with bacteria being finally released from infection threads into membrane-confined symbiosomes. We found that mutations in the symbiosis-specific SYMREM1 gene result in highly disorganized perimicrobial membranes. AlphaFold modelling and biochemical analyses reveal that SYMREM1 oligomerizes into antiparallel dimers and may form a higher-order membrane scaffolding structure. This was experimentally confirmed when expressing this and other remorins in wall-less protoplasts is sufficient where they significantly alter and stabilize de novo membrane topologies ranging from membrane blebs to long membrane tubes with a central actin filament. Reciprocally, mechanically induced membrane indentations were equally stabilized by SYMREM1. Taken together we describe a plant-specific mechanism that allows the stabilization of large-scale membrane conformations independent of the cell wall. |
format | Online Article Text |
id | pubmed-9852587 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-98525872023-01-21 Stabilization of membrane topologies by proteinaceous remorin scaffolds Su, Chao Rodriguez-Franco, Marta Lace, Beatrice Nebel, Nils Hernandez-Reyes, Casandra Liang, Pengbo Schulze, Eija Mymrikov, Evgeny V. Gross, Nikolas M. Knerr, Julian Wang, Hong Siukstaite, Lina Keller, Jean Libourel, Cyril Fischer, Alexandra A. M. Gabor, Katharina E. Mark, Eric Popp, Claudia Hunte, Carola Weber, Wilfried Wendler, Petra Stanislas, Thomas Delaux, Pierre-Marc Einsle, Oliver Grosse, Robert Römer, Winfried Ott, Thomas Nat Commun Article In plants, the topological organization of membranes has mainly been attributed to the cell wall and the cytoskeleton. Additionally, few proteins, such as plant-specific remorins have been shown to function as protein and lipid organizers. Root nodule symbiosis requires continuous membrane re-arrangements, with bacteria being finally released from infection threads into membrane-confined symbiosomes. We found that mutations in the symbiosis-specific SYMREM1 gene result in highly disorganized perimicrobial membranes. AlphaFold modelling and biochemical analyses reveal that SYMREM1 oligomerizes into antiparallel dimers and may form a higher-order membrane scaffolding structure. This was experimentally confirmed when expressing this and other remorins in wall-less protoplasts is sufficient where they significantly alter and stabilize de novo membrane topologies ranging from membrane blebs to long membrane tubes with a central actin filament. Reciprocally, mechanically induced membrane indentations were equally stabilized by SYMREM1. Taken together we describe a plant-specific mechanism that allows the stabilization of large-scale membrane conformations independent of the cell wall. Nature Publishing Group UK 2023-01-19 /pmc/articles/PMC9852587/ /pubmed/36658193 http://dx.doi.org/10.1038/s41467-023-35976-5 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 Su, Chao Rodriguez-Franco, Marta Lace, Beatrice Nebel, Nils Hernandez-Reyes, Casandra Liang, Pengbo Schulze, Eija Mymrikov, Evgeny V. Gross, Nikolas M. Knerr, Julian Wang, Hong Siukstaite, Lina Keller, Jean Libourel, Cyril Fischer, Alexandra A. M. Gabor, Katharina E. Mark, Eric Popp, Claudia Hunte, Carola Weber, Wilfried Wendler, Petra Stanislas, Thomas Delaux, Pierre-Marc Einsle, Oliver Grosse, Robert Römer, Winfried Ott, Thomas Stabilization of membrane topologies by proteinaceous remorin scaffolds |
title | Stabilization of membrane topologies by proteinaceous remorin scaffolds |
title_full | Stabilization of membrane topologies by proteinaceous remorin scaffolds |
title_fullStr | Stabilization of membrane topologies by proteinaceous remorin scaffolds |
title_full_unstemmed | Stabilization of membrane topologies by proteinaceous remorin scaffolds |
title_short | Stabilization of membrane topologies by proteinaceous remorin scaffolds |
title_sort | stabilization of membrane topologies by proteinaceous remorin scaffolds |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9852587/ https://www.ncbi.nlm.nih.gov/pubmed/36658193 http://dx.doi.org/10.1038/s41467-023-35976-5 |
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