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 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
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:	http://www.scopus.com/inward/record.url?...
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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