Current perspective on protein S-acylation in plants: more than just a fatty anchor?
Membranes are an important signalling platform in plants. The plasma membrane is the point where information about the external environment must be converted into intracellular signals, while endomembranes are important sites of protein trafficking, organization, compartmentalization, and intracellular signalling. This requires co-ordinating the spatial distribution of proteins, their activation state, and their interacting partners. This regulation frequently occurs through post-translational modification of proteins. Proteins that associate with the cell membrane do so through transmembrane domains, protein-protein interactions, lipid binding motifs/domains or use the post-translational addition of lipid groups as prosthetic membrane anchors. S-acylation is one such lipid modification capable of anchoring proteins to the membrane. Our current knowledge of S-acylation function in plants is fairly limited compared with other post-translational modifications and S-acylation in other organisms. However, it is becoming increasingly clear that S-acylation can act as more than just a simple membrane anchor: it can also act as a regulatory mechanism in signalling pathways in plants. S-acylation is, therefore, an ideal mechanism for regulating protein function at membranes. This review discusses our current knowledge of S-acylated proteins in plants, the interaction of different lipid modifications, and the general effects of S-acylation on cellular function.
Division of Plant Sciences, University of Dundee, The James Hutton Institute, Invergowrie, Dundee DD2 5DA, uk Cell and molecular sciences, The James Hutton Institute, Invergowrie, Dundee DD2 5DA, K.
Charlotte H
CH
Hurst
Division of Plant Sciences, University of Dundee, The James Hutton Institute, Invergowrie, Dundee DD2 5DA, uk Cell and molecular sciences, The James Hutton Institute, Invergowrie, Dundee DD2 5DA, K p.a.hemsley@dundee.ac.uk.
Piers A
http://orcid.org/0000-0003-2950-0634
PA
Hemsley
D000215:Acylation; D050356:Lipid Metabolism; D010940:Plant Proteins / Q000378:metabolism*; D010944:Plants / Q000378:metabolism*; D011499:Protein Processing, Post-Translational
D010940:Plant Proteins
Acylation; S-acylation.; lipid raft; lipidation; lipids; membrane; microdomain; palmitoylation; plant; post-translational modification