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Proteomic Analysis of a Poplar Cell Suspension Culture Suggests a Major Role of Protein S-Acylation in Diverse Cellular Processes
KTH, School of Biotechnology (BIO), Glycoscience.
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2016 (English)In: Frontiers in Plant Science, ISSN 1664-462X, E-ISSN 1664-462X, Vol. 7, 477Article in journal (Refereed) PublishedText
Abstract [en]

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.

Place, publisher, year, edition, pages
Frontiers media , 2016. Vol. 7, 477
Keyword [en]
poplar, post-translational modification, S-acylation, palmitoylation, massspectrometry, spectral counting
National Category
Biological Sciences
Identifiers
URN: urn:nbn:se:kth:diva-185971DOI: 10.3389/fpls.2016.00477ISI: 000373871500001ScopusID: 2-s2.0-84964284475OAI: oai:DiVA.org:kth-185971DiVA: diva2:926664
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QC 20160509

Available from: 2016-05-09 Created: 2016-04-29 Last updated: 2016-05-09Bibliographically approved

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