S-acylation stabilizes ligand-induced receptor kinase complex formation during plant pattern-triggered immune signaling

Hurst, Charlotte H; Turnbull, Dionne; Xhelilaj, Kaltra; Myles, Sally; Pflughaupt, Robin L; Kopischke, Michaela; Davies, Paul; Jones, Susan; Robatzek, Silke; Zipfel, Cyril; Gronnier, Julien; Hemsley, Piers A

doi:10.5167/uzh-233956

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Hurst, C. H., Turnbull, D., Xhelilaj, K., Myles, S., Pflughaupt, R. L., Kopischke, M., Davies, P., Jones, S., Robatzek, S., Zipfel, C., Gronnier, J., & Hemsley, P. A. (2023). S-acylation stabilizes ligand-induced receptor kinase complex formation during plant pattern-triggered immune signaling. Current Biology, 33(8), 1588-1596.e6. https://doi.org/10.1016/j.cub.2023.02.065

Abstract

Plant receptor kinases are key transducers of extracellular stimuli, such as the presence of beneficial or pathogenic microbes or secreted signaling molecules. Receptor kinases are regulated by numerous post-translationalmodifications. 1–3 Here, using the immune receptor kinases FLS24 and EFR,5 we show that S-acylation at a cysteine conserved in all plant receptor kinases is crucial for function. S-acylation involves the addition of long-chain fatty acids to cysteine residues within proteins, altering their biochemical properties and