%0 Journal Article
%T S-acylation stabilizes ligand-induced receptor kinase complex formation during plant pattern-triggered immune signaling.
%A Hurst CH
%A Turnbull D
%A Xhelilaj K
%A Myles S
%A Pflughaupt RL
%A Kopischke M
%A Davies P
%A Jones S
%A Robatzek S
%A Zipfel C
%A Gronnier J
%A Hemsley PA
%J Curr Biol
%V 33
%N 8
%D 04 2023 24
%M 36924767
%F 10.9
%R 10.1016/j.cub.2023.02.065
%X 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.