A proteomic approach identifies many novel palmitoylated proteins in Arabidopsis

Piers A. Hemsley*, Thilo Weimar, Kathryn S. Lilley, Paul Dupree, Claire S. Grierson

*Corresponding author for this work

Research output: Contribution to journalArticle (Academic Journal)peer-review

89 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)805-814
Number of pages10
JournalNew Phytologist
Volume197
Issue number3
DOIs
Publication statusPublished - Feb 2013

Keywords

  • Arabidopsis
  • FLS2
  • LRR-RLK
  • membrane
  • palmitoylation
  • pathogenesis
  • S-acylation
  • SNARE
  • PLASMA-MEMBRANE PROTEIN
  • S-ACYLATION
  • GENE FAMILY
  • PSEUDOMONAS-SYRINGAE
  • TIP GROWTH
  • FLAGELLIN PERCEPTION
  • GAMMA-SUBUNITS
  • RECEPTOR FLS2
  • PLANT DEFENSE
  • POLLEN-TUBE

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