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

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

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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-translational modifications.1,2,3 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 behavior within the membrane environment.6 We observe S-acylation of FLS2 at C-terminal kinase domain cysteine residues within minutes following the perception of its ligand, flg22, in a BAK1 co-receptor and PUB12/13 ubiquitin ligase-dependent manner. We demonstrate that S-acylation is essential for FLS2-mediated immune signaling and resistance to bacterial infection. Similarly, mutating the corresponding conserved cysteine residue in EFR suppressed elf18-triggered signaling. Analysis of unstimulated and activated FLS2-containing complexes using microscopy, detergents, and native membrane DIBMA nanodiscs indicates that S-acylation stabilizes, and promotes retention of, activated receptor kinase complexes at the plasma membrane to increase signaling efficiency.
Original languageEnglish
Pages (from-to)1588-1596.e6
Number of pages9
JournalCurrent Biology
Volume33
Issue number8
Early online date15 Mar 2023
DOIs
Publication statusPublished - 24 Apr 2023

Keywords

  • Arabidopsis
  • EFR
  • FLS2
  • S-acylation
  • microdomain
  • nanodomain
  • palmitoylation
  • plasma membrane
  • receptor kinase
  • receptor-like kinase

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