S-acylation stabilizes ligand-induced receptor kinase complex formation during plant pattern-triggered immune signalling Article Swipe
Charlotte H. Hurst
,
Dionne Turnbull
,
Kaltra Xhelilaj
,
Sally Myles
,
Robin L. Pflughaupt
,
Michaela Kopischke
,
Paul Davies
,
Susan R. Jones
,
Silke Robatzek
,
Cyril Zipfel
,
Julien Gronnier
,
Piers A. Hemsley
·
YOU?
·
· 2021
· Open Access
·
· DOI: https://doi.org/10.1101/2021.08.30.457756
YOU?
·
· 2021
· Open Access
·
· DOI: https://doi.org/10.1101/2021.08.30.457756
Summary Plant receptor kinases are key transducers of extracellular stimuli, such as the presence of beneficial or pathogenic microbes or secreted signalling molecules. Receptor kinases are regulated by numerous post-translational modifications. Here, using the immune receptor kinases FLS2 and EFR, 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 biophysical properties and behaviour within the membrane environment. We observe S-acylation of FLS2 at C-terminal kinase domain cysteine residues within minutes following perception of its ligand flg22, in a BAK1 co-receptor dependent manner. We demonstrate that S-acylation is essential for FLS2-mediated immune signalling and resistance to bacterial infection. Similarly, mutating the corresponding conserved cysteine residue in EFR supressed elf18 triggered signalling. Analysis of unstimulated and activated FLS2-containing complexes using microscopy, detergents and native membrane DIBMA nanodiscs indicates that S-acylation stabilises and promotes retention of activated receptor kinase complexes at the plasma membrane to increase signalling efficiency.
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- Type
- preprint
- Language
- en
- Landing Page
- https://doi.org/10.1101/2021.08.30.457756
- https://www.biorxiv.org/content/biorxiv/early/2022/03/07/2021.08.30.457756.full.pdf
- OA Status
- green
- References
- 78
- Related Works
- 10
- OpenAlex ID
- https://openalex.org/W3198447908
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Raw OpenAlex JSON
- OpenAlex ID
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https://openalex.org/W3198447908Canonical identifier for this work in OpenAlex
- DOI
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https://doi.org/10.1101/2021.08.30.457756Digital Object Identifier
- Title
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S-acylation stabilizes ligand-induced receptor kinase complex formation during plant pattern-triggered immune signallingWork title
- Type
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preprintOpenAlex work type
- Language
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enPrimary language
- Publication year
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2021Year of publication
- Publication date
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2021-08-31Full publication date if available
- Authors
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Charlotte H. Hurst, Dionne Turnbull, Kaltra Xhelilaj, Sally Myles, Robin L. Pflughaupt, Michaela Kopischke, Paul Davies, Susan R. Jones, Silke Robatzek, Cyril Zipfel, Julien Gronnier, Piers A. HemsleyList of authors in order
- Landing page
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https://doi.org/10.1101/2021.08.30.457756Publisher landing page
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https://www.biorxiv.org/content/biorxiv/early/2022/03/07/2021.08.30.457756.full.pdfDirect link to full text PDF
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YesWhether a free full text is available
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greenOpen access status per OpenAlex
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https://www.biorxiv.org/content/biorxiv/early/2022/03/07/2021.08.30.457756.full.pdfDirect OA link when available
- Concepts
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Kinase, Cysteine, Cell biology, Acylation, Biochemistry, Receptor, Chemistry, Extracellular, Biology, Enzyme, CatalysisTop concepts (fields/topics) attached by OpenAlex
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0Total citation count in OpenAlex
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78Number of works referenced by this work
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10Other works algorithmically related by OpenAlex
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