Journal
NEW PHYTOLOGIST
Volume 197, Issue 3, Pages 805-814Publisher
WILEY-BLACKWELL
DOI: 10.1111/nph.12077
Keywords
Arabidopsis; FLS2; LRR-RLK; membrane; palmitoylation; pathogenesis; S-acylation; SNARE
Categories
Funding
- Biotechnology and Biological Sciences Research Council (BBSRC) [BB/D013585/1]
- Lady Emily Smyth Agricultural Research Station
- BBSRC [BB/C507561/1]
- Biotechnology and Biological Sciences Research Council [BB/C507561/1, BB/D013585/1] Funding Source: researchfish
- BBSRC [BB/D013585/1] Funding Source: UKRI
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S-acylation (palmitoylation) is a poorly understood post-translational modification of proteins involving the addition of acyl lipids to cysteine residues. S-acylation promotes the association of proteins with membranes and influences protein stability, microdomain partitioning, membrane targeting and activation state. No consensus motif for S-acylation exists and it therefore requires empirical identification. Here, we describe a biotin switch isobaric tagging for relative and absolute quantification (iTRAQ)-based method to identify S-acylated proteins from Arabidopsis. We use these data to predict and confirm S-acylation of proteins not in our dataset. We identified c. 600 putative S-acylated proteins affecting diverse cellular processes. These included proteins involved in pathogen perception and response, mitogen-activated protein kinases (MAPKs), leucine-rich repeat receptor-like kinases (LRR-RLKs) and RLK superfamily members, integral membrane transporters, ATPases, soluble N-ethylmaleimide-sensitive factor-activating protein receptors (SNAREs) and heterotrimeric G-proteins. The prediction of S-acylation of related proteins was demonstrated by the identification and confirmation of S-acylation sites within the SNARE and LRR-RLK families. We showed that S-acylation of the LRR-RLK FLS2 is required for a full response to elicitation by the flagellin derived peptide flg22, but is not required for localization to the plasma membrane. Arabidopsis contains many more S-acylated proteins than previously thought. These data can be used to identify S-acylation sites in related proteins. We also demonstrated that S-acylation is required for full LRR-RLK function.
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