Back to Search
Start Over
Proteomic Analysis of a Poplar Cell Suspension Culture Suggests a Major Role of Protein S-Acylation in Diverse Cellular Processes.
- Source :
-
Frontiers in plant science [Front Plant Sci] 2016 Apr 12; Vol. 7, pp. 477. Date of Electronic Publication: 2016 Apr 12 (Print Publication: 2016). - Publication Year :
- 2016
-
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.
Details
- Language :
- English
- ISSN :
- 1664-462X
- Volume :
- 7
- Database :
- MEDLINE
- Journal :
- Frontiers in plant science
- Publication Type :
- Academic Journal
- Accession number :
- 27148305
- Full Text :
- https://doi.org/10.3389/fpls.2016.00477