Hurst, Charlotte H., Turnbull, Dionne, Xhelilaj, Kaltra, Myles, Sally, Pflughaupt, Robin L., Kopischke, Michaela, Davies, Paul, Jones, Susan, Robatzek, Silke, Zipfel, Cyril, Gronnier, Julien and Hemsley, Piers A. (2023) S-acylation stabilizes ligand-induced receptor kinase complex formation during plant pattern-triggered immune signaling. Current Biology, 33 (8). 1588-1596.e6. ISSN 0960-9822
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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.
Item Type: | Article |
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Additional Information: | Funding Information: This work was supported by BBSRC EASTBIO-DTP studentship (grant number BB/M010996/1) to S.M. and P.A.H., BBSRC grants BB/M024911/1 and BB/P007902/1 to P.A.H., Royal Society grant RG140531 to P.A.H., a Heisenberg fellowship from the Deutsche Forschungsgemeinschaft to S.R., the Gatsby Charitable Foundation, the University of Zürich, the European Research Council (grant agreement 773153 IMMUNO-PEPTALK) to C.Z., the European Molecular Biology Organization (EMBO Long-Term Fellowship 438 - 2018 ), and the German Research Foundation (DFG grant CRC1101-A09 ) to J.G. S.J. was supported by the Scottish Government’s Rural and Environment Science and Analytical Services Division (RESAS). |
Uncontrolled Keywords: | arabidopsis,efr,fls2,s-acylation,microdomain,nanodomain,palmitoylation,plasma membrane,receptor kinase,receptor-like kinase,neuroscience(all),biochemistry, genetics and molecular biology(all),agricultural and biological sciences(all) ,/dk/atira/pure/subjectarea/asjc/2800 |
Faculty \ School: | Faculty of Science > The Sainsbury Laboratory Faculty of Science > School of Biological Sciences |
UEA Research Groups: | Faculty of Science > Research Groups > Plant Sciences |
Related URLs: | |
Depositing User: | LivePure Connector |
Date Deposited: | 21 Mar 2023 09:35 |
Last Modified: | 28 Apr 2023 08:30 |
URI: | https://ueaeprints.uea.ac.uk/id/eprint/91626 |
DOI: | 10.1016/j.cub.2023.02.065 |
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