{Reference Type}: Journal Article
{Title}: S-acylation stabilizes ligand-induced receptor kinase complex formation during plant pattern-triggered immune signaling.
{Author}: Hurst CH;Turnbull D;Xhelilaj K;Myles S;Pflughaupt RL;Kopischke M;Davies P;Jones S;Robatzek S;Zipfel C;Gronnier J;Hemsley PA;
{Journal}: Curr Biol
{Volume}: 33
{Issue}: 8
{Year}: 04 2023 24
{Factor}: 10.9
{DOI}: 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-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.