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Front Plant Sci. 2016 Apr 12;7:477. doi: 10.3389/fpls.2016.00477. eCollection 2016.

Proteomic Analysis of a Poplar Cell Suspension Culture Suggests a Major Role of Protein S-Acylation in Diverse Cellular Processes.

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Division of Glycoscience, School of Biotechnology, Royal Institute of Technology, AlbaNova University Centre Stockholm, Sweden.
Roy J. Carver Biotechnology Centre, Institute for Genomic Biology, University of Illinois Urbana-Champaign Urbana, IL, USA.
Division of Glycoscience, School of Biotechnology, Royal Institute of Technology, AlbaNova University CentreStockholm, Sweden; ARC Centre of Excellence in Plant Cell Walls and School of Agriculture, Food and Wine, The University of Adelaide, Waite CampusUrrbrae, SA, Australia.


S-acylation is a reversible post-translational modification of proteins known to be involved in membrane targeting, subcellular trafficking, and the determination of a great variety of functional properties of proteins. The aim of this work was to identify S-acylated proteins in poplar. The use of an acyl-biotin exchange method and mass spectrometry allowed the identification of around 450 S-acylated proteins, which were subdivided into three major groups of proteins involved in transport, signal transduction, and response to stress, respectively. The largest group of S-acylated proteins was the protein kinase superfamily. Soluble N-ethylmaleimide-sensitive factor-activating protein receptors, band 7 family proteins and tetraspanins, all primarily related to intracellular trafficking, were also identified. In addition, cell wall related proteins, including cellulose synthases and other glucan synthases, were found to be S-acylated. Twenty four of the identified S-acylated proteins were also enriched in detergent-resistant membrane microdomains, suggesting S-acylation plays a key role in the localization of proteins to specialized plasma membrane subdomains. This dataset promises to enhance our current understanding of the various functions of S-acylated proteins in plants.


S-acylation; mass spectrometry; palmitoylation; poplar; post-translational modification; spectral counting

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