Proteomic analysis of a poplar cell suspension culture suggests a major role of protein S-acylation in diverse cellular processes

Frontiers in Plant Science

Erik eMalm¹  Vaibhav eSrivastava¹  Vincent eBulone²  Joseph R. Weber³  Bruce William Fouke³ 

[1] Royal Institute of Technology, KTH;The University of Adelaide;University of Illinois Urbana-Champaign;

关键词: Mass Spectrometry;    poplar;    palmitoylation;    post-translational modification;    spectral counting;    S-Acylation;   

DOI  :  10.3389/fpls.2016.00477

来源: DOAJ

【 摘 要 】

S-acylation is a reversible post-translational modification (PTM) 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. Th 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 (SNAREs), 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.

【 授权许可】

Unknown