Regulation of immune receptor kinase plasma membrane nanoscale organization by a plant peptide hormone and its receptors

• Published in: eLife Vol. 11
• Main Authors: 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
• Format: Journal Article
• Language: English
• Published: England eLife Sciences Publications Ltd 06.01.2022; eLife Sciences Publications, Ltd
• Subjects: Arabidopsis - genetics; Arabidopsis - metabolism; Arabidopsis Proteins - genetics; Arabidopsis Proteins - metabolism; Cell Biology; Cell surface; Clustering; Experiments; Extensin; Flagellin; innate immunity; Kinases; Ligands; Microscopy; nanoscale organization; peptide hormones; Peptides; Perception; Phosphotransferases - genetics; Phosphotransferases - metabolism; Plant Biology; Plant Immunity - genetics; Plasma; plasma membrane; Protein Kinases - genetics; Protein Kinases - metabolism; Protein Serine-Threonine Kinases - genetics; Protein Serine-Threonine Kinases - metabolism; Proteins; receptor kinase; signaling; cell biology; peptide hormones; signaling; innate immunity; plasma membrane; A. thaliana; nanoscale organization; plant biology; receptor kinase
• ISSN: 2050-084X; 2050-084X
• DOI: 10.7554/eLife.74162

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.