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

Vaibhav Srivastava, Joseph R. Weber, Erik Malm, Bruce W. Fouke, Vincent Bulone

Research output: Contribution to journalArticlepeer-review

20 Citations (Scopus)
1 Downloads (Pure)

Abstract

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.

Original languageEnglish
Article number477
Number of pages11
JournalFrontiers in Plant Science
Volume7
DOIs
Publication statusPublished - 12 Apr 2016
Externally publishedYes

Keywords

  • Mass spectrometry
  • Palmitoylation
  • Poplar
  • Post-translational modification
  • S-acylation
  • Spectral counting

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