Institute of Plant and Microbial Biology and Zurich-Basel Plant Science Center, University of Zurich, Zurich, Switzerland; The Sainsbury Laboratory, University of East Anglia, Norwich Research Park, Norwich, United Kingdom
Christina M Franck
Institute of Plant and Microbial Biology and Zurich-Basel Plant Science Center, University of Zurich, Zurich, Switzerland
Martin Stegmann
The Sainsbury Laboratory, University of East Anglia, Norwich Research Park, Norwich, United Kingdom
Thomas A DeFalco
Institute of Plant and Microbial Biology and Zurich-Basel Plant Science Center, University of Zurich, Zurich, Switzerland; The Sainsbury Laboratory, University of East Anglia, Norwich Research Park, Norwich, United Kingdom
Institute of Plant and Microbial Biology and Zurich-Basel Plant Science Center, University of Zurich, Zurich, Switzerland
Michelle von Arx
Institute of Plant and Microbial Biology and Zurich-Basel Plant Science Center, University of Zurich, Zurich, Switzerland
Kai Dünser
Department of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences Vienna, Vienna, Austria
Wenwei Lin
FAFU-UCR Joint Center for Horticultural Biology and Metabolomics Center, Haixia, Institute of Science and Technology, Fujian Agriculture and Forestry University, Fuzhou, China
Zhenbiao Yang
FAFU-UCR Joint Center for Horticultural Biology and Metabolomics Center, Haixia, Institute of Science and Technology, Fujian Agriculture and Forestry University, Fuzhou, China
Institute of Plant and Microbial Biology and Zurich-Basel Plant Science Center, University of Zurich, Zurich, Switzerland; The Sainsbury Laboratory, University of East Anglia, Norwich Research Park, Norwich, United Kingdom
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.
