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

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; Zipfel, Cyril

doi:10.5167/uzh-207239

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Bender, K. W., Couto, D., Kadota, Y., Macho, A. P., Sklenar, J., Derbyshire, P., Bjornson, M., DeFalco, T. A., Petriello, A., Font Farre, M., Schwessinger, B., Ntoukakis, V., Stransfeld, L., Jones, A. M. E., Menke, F. L. H., & Zipfel, C. (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. https://doi.org/10.1073/pnas.2108242118

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 ch