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231224s2013 xx |||||o 00| ||eng c |
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|a 10.1111/nph.12077
|2 doi
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|a pubmed24n0745.xml
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|a (DE-627)NLM223560448
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|a (NLM)23252521
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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|a Hemsley, Piers A
|e verfasserin
|4 aut
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|a A proteomic approach identifies many novel palmitoylated proteins in Arabidopsis
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|c 2013
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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|a ƒa Online-Ressource
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|2 rdacarrier
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|a Date Completed 21.06.2013
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|a Date Revised 16.04.2021
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a © 2012 The Authors. New Phytologist © 2012 New Phytologist Trust.
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|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
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Arabidopsis Proteins
|2 NLM
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|a SNARE Proteins
|2 NLM
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|a Acyltransferases
|2 NLM
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|a EC 2.3.-
|2 NLM
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|a TIP1 protein, Arabidopsis
|2 NLM
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|a EC 2.3.1.-
|2 NLM
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|a Weimar, Thilo
|e verfasserin
|4 aut
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|a Lilley, Kathryn S
|e verfasserin
|4 aut
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|a Dupree, Paul
|e verfasserin
|4 aut
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|a Grierson, Claire S
|e verfasserin
|4 aut
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|i Enthalten in
|t The New phytologist
|d 1979
|g 197(2013), 3 vom: 08. Feb., Seite 805-814
|w (DE-627)NLM09818248X
|x 1469-8137
|7 nnns
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|g volume:197
|g year:2013
|g number:3
|g day:08
|g month:02
|g pages:805-814
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|u http://dx.doi.org/10.1111/nph.12077
|3 Volltext
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|d 197
|j 2013
|e 3
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|c 02
|h 805-814
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