Publication: S-acylation stabilizes ligand-induced receptor kinase complex formation during plant pattern-triggered immune signalling
S-acylation stabilizes ligand-induced receptor kinase complex formation during plant pattern-triggered immune signalling
Date
Date
Date
Citations
Hurst, C. H., Turnbull, D., Xhelilaj, K., Myles, S., Pflughaupt, R. L., Kopischke, M., Davies, P., Jones, S., Robatzek, S., Zipfel, C., Gronnier, J., & Hemsley, P. A. (2023). S-acylation stabilizes ligand-induced receptor kinase complex formation during plant pattern-triggered immune signalling (No. 457756; BioRxiv). https://doi.org/10.1101/2021.08.30.457756
Abstract
Abstract
Abstract
SummaryPlant 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 a
Metrics
Downloads
Views
Additional indexing
Creators (Authors)
Series Name
Series Name
Series Name
Item Type
Item Type
Item Type
Language
Language
Language
Publication date
Publication date
Publication date
Date available
Date available
Date available
ISSN or e-ISSN
ISSN or e-ISSN
ISSN or e-ISSN
OA Status
OA Status
OA Status
Publisher DOI
Metrics
Downloads
Views
Citations
Hurst, C. H., Turnbull, D., Xhelilaj, K., Myles, S., Pflughaupt, R. L., Kopischke, M., Davies, P., Jones, S., Robatzek, S., Zipfel, C., Gronnier, J., & Hemsley, P. A. (2023). S-acylation stabilizes ligand-induced receptor kinase complex formation during plant pattern-triggered immune signalling (No. 457756; BioRxiv). https://doi.org/10.1101/2021.08.30.457756