Perception of a conserved family of plant signalling peptides by the receptor kinase HSL3
Abstract
Plant genomes encode hundreds of secreted peptides; however, relatively few have been characterised. We report here an uncharacterised, stress-induced family of plant signalling peptides, which we call CTNIPs. Based on the role of the common co-receptor BRASSINOSTEROID INSENSITIVE 1-ASSOCIATED KINASE 1 (BAK1) in CTNIP-induced responses, we identified in Arabidopsis thaliana the orphan receptor kinase HAESA-LIKE 3 (HSL3) as the CTNIP receptor via a proteomics approach. CTNIP binding, ligand-triggered complex formation with BAK1, and induced downstream responses all involve HSL3. Notably, the HSL3-CTNIP signalling module is evolutionarily conserved amongst most extant angiosperms. The identification of this novel signalling module will further shed light on the diverse functions played by plant signalling peptides and will provide insights into receptor-ligand co-evolution.
Data availability
The mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium via the PRIDE (Perez-Riverol et al., 2016) partner repository with the dataset identifier PXD029264 and 10.6019/PXD029264The RNA-seq datasets generated and analysed in the current study have been deposited in the ArrayExpress database at EMBL-EBI (www.ebi.ac.uk/arrayexpress) under accession number E-MTAB-11093.
Article and author information
Author details
Funding
H2020 European Research Council (773153)
- Cyril Zipfel
H2020 European Research Council (716358)
- Julia Santiago
The Gatsby Charitable Foundation
- Cyril Zipfel
Universität Zürich
- Cyril Zipfel
Swiss National Science Foundation (31003A_182625)
- Cyril Zipfel
Swiss National Science Foundation (31003A_173101)
- Julia Santiago
Fondation philanthropique Famille Sandoz
- Julia Santiago
H2020 Marie Skłodowska-Curie Actions (703954)
- Marta Bjornson
Biotechnology and Biological Sciences Research Council (BB/P012574/1)
- Cyril Zipfel
The funders had no role in study design, data collection and interpretation, or the decision to submit the work for publication.
Reviewing Editor
- Caroline Gutjahr, Technical University of Munich, Germany
Version history
- Received: October 13, 2021
- Preprint posted: October 26, 2021 (view preprint)
- Accepted: May 26, 2022
- Accepted Manuscript published: May 26, 2022 (version 1)
- Version of Record published: June 13, 2022 (version 2)
Copyright
© 2022, Rhodes et al.
This article is distributed under the terms of the Creative Commons Attribution License permitting unrestricted use and redistribution provided that the original author and source are credited.
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Further reading
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- Microbiology and Infectious Disease
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Purinergic signaling activated by extracellular nucleotides and their derivative nucleosides trigger sophisticated signaling networks. The outcome of these pathways determine the capacity of the organism to survive under challenging conditions. Both extracellular ATP (eATP) and Adenosine (eAdo) act as primary messengers in mammals, essential for immunosuppressive responses. Despite the clear role of eATP as a plant damage-associated molecular pattern, the function of its nucleoside, eAdo, and of the eAdo/eATP balance in plant stress response remain to be fully elucidated. This is particularly relevant in the context of plant-microbe interaction, where the intruder manipulates the extracellular matrix. Here, we identify Ado as a main molecule secreted by the vascular fungus Fusarium oxysporum. We show that eAdo modulates the plant's susceptibility to fungal colonization by altering the eATP-mediated apoplastic pH homeostasis, an essential physiological player during the infection of this pathogen. Our work indicates that plant pathogens actively imbalance the apoplastic eAdo/eATP levels as a virulence mechanism.
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