A proteomic approach identifies many novel palmitoylated proteins in Arabidopsis

© 2012 The Authors. New Phytologist © 2012 New Phytologist Trust.

Bibliographische Detailangaben
Veröffentlicht in:The New phytologist. - 1979. - 197(2013), 3 vom: 08. Feb., Seite 805-814
1. Verfasser: Hemsley, Piers A (VerfasserIn)
Weitere Verfasser: Weimar, Thilo, Lilley, Kathryn S, Dupree, Paul, Grierson, Claire S
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2013
Zugriff auf das übergeordnete Werk:The New phytologist
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Arabidopsis Proteins SNARE Proteins Acyltransferases EC 2.3.- TIP1 protein, Arabidopsis EC 2.3.1.-
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520 |a 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 
650 4 |a Journal Article 
650 4 |a Research Support, Non-U.S. Gov't 
650 7 |a Arabidopsis Proteins  |2 NLM 
650 7 |a SNARE Proteins  |2 NLM 
650 7 |a Acyltransferases  |2 NLM 
650 7 |a EC 2.3.-  |2 NLM 
650 7 |a TIP1 protein, Arabidopsis  |2 NLM 
650 7 |a EC 2.3.1.-  |2 NLM 
700 1 |a Weimar, Thilo  |e verfasserin  |4 aut 
700 1 |a Lilley, Kathryn S  |e verfasserin  |4 aut 
700 1 |a Dupree, Paul  |e verfasserin  |4 aut 
700 1 |a Grierson, Claire S  |e verfasserin  |4 aut 
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773 1 8 |g volume:197  |g year:2013  |g number:3  |g day:08  |g month:02  |g pages:805-814 
856 4 0 |u http://dx.doi.org/10.1111/nph.12077  |3 Volltext 
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