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Regulation of immune receptor kinase plasma membrane nanoscale organization by a plant peptide hormone and its receptors
Spatial partitioning is a propensity of biological systems orchestrating cell activities in space and time. The dynamic regulation of plasma membrane nano-environments has recently emerged as a key fundamental aspect of plant signaling, but the molecular components governing it are still mostly uncl...
Autores principales: | , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
eLife Sciences Publications, Ltd
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8791635/ https://www.ncbi.nlm.nih.gov/pubmed/34989334 http://dx.doi.org/10.7554/eLife.74162 |
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author | Gronnier, Julien Franck, Christina M Stegmann, Martin DeFalco, Thomas A Abarca, Alicia von Arx, Michelle Dünser, Kai Lin, Wenwei Yang, Zhenbiao Kleine-Vehn, Jürgen Ringli, Christoph Zipfel, Cyril |
author_facet | Gronnier, Julien Franck, Christina M Stegmann, Martin DeFalco, Thomas A Abarca, Alicia von Arx, Michelle Dünser, Kai Lin, Wenwei Yang, Zhenbiao Kleine-Vehn, Jürgen Ringli, Christoph Zipfel, Cyril |
author_sort | Gronnier, Julien |
collection | PubMed |
description | Spatial partitioning is a propensity of biological systems orchestrating cell activities in space and time. The dynamic regulation of plasma membrane nano-environments has recently emerged as a key fundamental aspect of plant signaling, but the molecular components governing it are still mostly unclear. The receptor kinase FERONIA (FER) controls ligand-induced complex formation of the immune receptor kinase FLAGELLIN SENSING 2 (FLS2) with its co-receptor BRASSINOSTEROID-INSENSITIVE 1-ASSOCIATED KINASE 1 (BAK1), and perception of the endogenous peptide hormone RAPID ALKALANIZATION FACTOR 23 (RALF23) by FER inhibits immunity. Here, we show that FER regulates the plasma membrane nanoscale organization of FLS2 and BAK1. Our study demonstrates that akin to FER, leucine-rich repeat (LRR) extensin proteins (LRXs) contribute to RALF23 responsiveness and regulate BAK1 nanoscale organization and immune signaling. Furthermore, RALF23 perception leads to rapid modification of FLS2 and BAK1 nanoscale organization, and its inhibitory activity on immune signaling relies on FER kinase activity. Our results suggest that perception of RALF peptides by FER and LRXs actively modulates plasma membrane nanoscale organization to regulate cell surface signaling by other ligand-binding receptor kinases. |
format | Online Article Text |
id | pubmed-8791635 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | eLife Sciences Publications, Ltd |
record_format | MEDLINE/PubMed |
spelling | pubmed-87916352022-01-27 Regulation of immune receptor kinase plasma membrane nanoscale organization by a plant peptide hormone and its receptors Gronnier, Julien Franck, Christina M Stegmann, Martin DeFalco, Thomas A Abarca, Alicia von Arx, Michelle Dünser, Kai Lin, Wenwei Yang, Zhenbiao Kleine-Vehn, Jürgen Ringli, Christoph Zipfel, Cyril eLife Cell Biology Spatial partitioning is a propensity of biological systems orchestrating cell activities in space and time. The dynamic regulation of plasma membrane nano-environments has recently emerged as a key fundamental aspect of plant signaling, but the molecular components governing it are still mostly unclear. The receptor kinase FERONIA (FER) controls ligand-induced complex formation of the immune receptor kinase FLAGELLIN SENSING 2 (FLS2) with its co-receptor BRASSINOSTEROID-INSENSITIVE 1-ASSOCIATED KINASE 1 (BAK1), and perception of the endogenous peptide hormone RAPID ALKALANIZATION FACTOR 23 (RALF23) by FER inhibits immunity. Here, we show that FER regulates the plasma membrane nanoscale organization of FLS2 and BAK1. Our study demonstrates that akin to FER, leucine-rich repeat (LRR) extensin proteins (LRXs) contribute to RALF23 responsiveness and regulate BAK1 nanoscale organization and immune signaling. Furthermore, RALF23 perception leads to rapid modification of FLS2 and BAK1 nanoscale organization, and its inhibitory activity on immune signaling relies on FER kinase activity. Our results suggest that perception of RALF peptides by FER and LRXs actively modulates plasma membrane nanoscale organization to regulate cell surface signaling by other ligand-binding receptor kinases. eLife Sciences Publications, Ltd 2022-01-06 /pmc/articles/PMC8791635/ /pubmed/34989334 http://dx.doi.org/10.7554/eLife.74162 Text en © 2022, Gronnier et al https://creativecommons.org/licenses/by/4.0/This article is distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use and redistribution provided that the original author and source are credited. |
spellingShingle | Cell Biology Gronnier, Julien Franck, Christina M Stegmann, Martin DeFalco, Thomas A Abarca, Alicia von Arx, Michelle Dünser, Kai Lin, Wenwei Yang, Zhenbiao Kleine-Vehn, Jürgen Ringli, Christoph Zipfel, Cyril Regulation of immune receptor kinase plasma membrane nanoscale organization by a plant peptide hormone and its receptors |
title | Regulation of immune receptor kinase plasma membrane nanoscale organization by a plant peptide hormone and its receptors |
title_full | Regulation of immune receptor kinase plasma membrane nanoscale organization by a plant peptide hormone and its receptors |
title_fullStr | Regulation of immune receptor kinase plasma membrane nanoscale organization by a plant peptide hormone and its receptors |
title_full_unstemmed | Regulation of immune receptor kinase plasma membrane nanoscale organization by a plant peptide hormone and its receptors |
title_short | Regulation of immune receptor kinase plasma membrane nanoscale organization by a plant peptide hormone and its receptors |
title_sort | regulation of immune receptor kinase plasma membrane nanoscale organization by a plant peptide hormone and its receptors |
topic | Cell Biology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8791635/ https://www.ncbi.nlm.nih.gov/pubmed/34989334 http://dx.doi.org/10.7554/eLife.74162 |
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