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Activation loop phosphorylaton of a non-RD receptor kinase initiates plant innate immune signaling

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Bender, Kyle W., Couto, Daniel, Kadota, Yasuhiro, Macho, Alberto P., Sklenar, Jan, Derbyshire, Paul, Bjornson, Marta, DeFalco, Thomas A., Petriello, Annalise, Font Farre, Maria, Schwessinger, Benjamin, Ntoukakis, Vardis, Stransfeld, Lena, Jones, Alexandra M. E., Menke, Frank L. H. and Zipfel, Cyril (2021) Activation loop phosphorylaton of a non-RD receptor kinase initiates plant innate immune signaling. Proceedings of the National Academy of Sciences of the United States of America, 118 (38). e2108242118. doi:10.1073/pnas.2108242118 ISSN 0027-8424.

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Official URL: http://dx.doi.org/10.1073/pnas.2108242118

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Abstract

Receptor kinases (RKs) are fundamental for extracellular sensing and regulate development and stress responses across kingdoms. In plants, leucine-rich repeat receptor kinases (LRR-RKs) are primarily peptide receptors that regulate responses to myriad internal and external stimuli. Phosphorylation of LRR-RK cytoplasmic domains is among the earliest responses following ligand perception, and reciprocal transphosphorylation between a receptor and its coreceptor is thought to activate the receptor complex. Originally proposed based on characterization of the brassinosteroid receptor, the prevalence of complex activation via reciprocal transphosphorylation across the plant RK family has not been tested. Using the LRR-RK ELONGATION FACTOR TU RECEPTOR (EFR) as a model, we set out to understand the steps critical for activating RK complexes. While the EFR cytoplasmic domain is an active protein kinase in vitro and is phosphorylated in a ligand-dependent manner in vivo, catalytically deficient EFR variants are functional in antibacterial immunity. These results reveal a noncatalytic role for EFR in triggering immune signaling and indicate that reciprocal transphoshorylation is not a ubiquitous requirement for LRR-RK complex activation. Rather, our analysis of EFR along with a detailed survey of the literature suggests a distinction between LRR-RKs with RD- versus non-RD protein kinase domains. Based on newly identified phosphorylation sites that regulate the activation state of the EFR complex in vivo, we propose that LRR-RK complexes containing a non-RD protein kinase may be regulated by phosphorylation-dependent conformational changes of the ligand-binding receptor, which could initiate signaling either allosterically or through driving the dissociation of negative regulators of the complex.

Item Type: Journal Article
Subjects: Q Science > QK Botany
Q Science > QP Physiology
S Agriculture > SB Plant culture
Divisions: Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- )
Library of Congress Subject Headings (LCSH): Plants -- Phosphorylation, Plant immunology, Plant cellular signal transduction, Protein kinases
Journal or Publication Title: Proceedings of the National Academy of Sciences of the United States of America
Publisher: National Academy of Sciences
ISSN: 0027-8424
Official Date: 2021
Dates:
DateEvent
2021Published
16 September 2021Available
4 August 2021Accepted
Volume: 118
Number: 38
Article Number: e2108242118
DOI: 10.1073/pnas.2108242118
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Open Access (Creative Commons)
Date of first compliant deposit: 21 September 2021
Date of first compliant Open Access: 21 September 2021
RIOXX Funder/Project Grant:
Project/Grant IDRIOXX Funder NameFunder ID
UNSPECIFIEDGatsby Charitable Foundationhttp://dx.doi.org/10.13039/501100000324
BB/P012574/1[BBSRC] Biotechnology and Biological Sciences Research Councilhttp://dx.doi.org/10.13039/501100000268
PHOSPHinnATE / 309858H2020 European Research Councilhttp://dx.doi.org/10.13039/100010663
IMMUNO-PEPTALK / 773153H2020 European Research Councilhttp://dx.doi.org/10.13039/100010663
UNSPECIFIEDUniversität Zürichhttp://viaf.org/viaf/122255956
31003A_182625[SNSF] Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschunghttp://dx.doi.org/10.13039/501100001711
BB/S004734/1UK Research and Innovationhttp://dx.doi.org/10.13039/100014013
UNSPECIFIEDRIKENhttp://dx.doi.org/10.13039/501100006264
UNSPECIFIEDUehara Memorial Foundationhttp://dx.doi.org/10.13039/100008732
703954[ERC] Horizon 2020 Framework Programmehttp://dx.doi.org/10.13039/100010661
Sainsbury Laboratory PhD Rotation ProgramJohn Innes Foundationhttp://dx.doi.org/10.13039/501100004034
EMBO LTF 100-2017European Molecular Biology Organizationhttp://dx.doi.org/10.13039/100004410
NSERC PDF-532561-2019[NSERC] Natural Sciences and Engineering Research Council of Canadahttp://dx.doi.org/10.13039/501100000038

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