A Bacterial Tyrosine Phosphatase Inhibits Plant Pattern Recognition Receptor Activation

Macho, Alberto P; Schwessinger, Benjamin; Ntoukakis, Vardis; Brutus, Alexandre; Segonzac, Cécile; Roy, Sonali; Kadota, Yasuhiro; Oh, Man-Ho; Sklenar, Jan; Derbyshire, Paul; Lozano-Durán, Rosa; Malinovsky, Frederikke Gro; Monaghan, Jacqueline; Menke, Frank L H; Huber, Steven C; He, Sheng Yang; Zipfel, Cyril

doi:10.5167/uzh-260343

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Macho, A. P., Schwessinger, B., Ntoukakis, V., Brutus, A., Segonzac, C., Roy, S., Kadota, Y., Oh, M.-H., Sklenar, J., Derbyshire, P., Lozano-Durán, R., Malinovsky, F. G., Monaghan, J., Menke, F. L. H., Huber, S. C., He, S. Y., & Zipfel, C. (2014). A Bacterial Tyrosine Phosphatase Inhibits Plant Pattern Recognition Receptor Activation. Science, 343(6178), 1509–1512. https://doi.org/10.1126/science.1248849

Abstract

Innate immunity relies on the perception of pathogen-associated molecular patterns (PAMPs) by pattern-recognition receptors (PRRs) located on the host cell's surface. Many plant PRRs are kinases. Here, we report that the Arabidopsis receptor kinase EF-TU RECEPTOR (EFR), which perceives the elf18 peptide derived from bacterial elongation factor Tu, is activated upon ligand binding by phosphorylation on its tyrosine residues. Phosphorylation of a single tyrosine residue, Y836, is required for activation of EFR and downstream immunity to