Progress toward Understanding Protein S-acylation: Prospective in Plants.

Yaxiao Li,Baoxiu Qi

doi:10.3389/fpls.2017.00346

Abstract

S-acylation, also known as S-palmitoylation or palmitoylation, is a reversible post-translational lipid modification in which long chain fatty acid, usually the 16-carbon palmitate, covalently attaches to a cysteine residue(s) throughout the protein via a thioester bond. It is involved in an array of important biological processes during growth and development, reproduction and stress responses in plant. S-acylation is a ubiquitous mechanism in eukaryotes catalyzed by a family of enzymes called Protein S-Acyl Transferases (PATs). Since the discovery of the first PAT in yeast in 2002 research in S-acylation has accelerated in the mammalian system and followed by in plant. However, it is still a difficult field to study due to the large number of PATs and even larger number of putative S-acylated substrate proteins they modify in each genome. This is coupled with drawbacks in the techniques used to study S-acylation, leading to the slower progress in this field compared to protein phosphorylation, for example. In this review we will summarize the discoveries made so far based on knowledge learnt from the characterization of protein S-acyltransferases and the S-acylated proteins, the interaction mechanisms between PAT and its specific substrate protein(s) in yeast and mammals. Research in protein S-acylation and PATs in plants will also be covered although this area is currently less well studied in yeast and mammalian systems.

Highlights

Lipid modification is a common mechanism in organisms, in which a fatty acid attaches to specific amino acid residues, leading to increased hydrophobicity of proteins which aids their anchoring to membranes or specific lipid rafts (Levental et al, 2010)
Ever since the discovery of the first S-acyltransferase, Akr1 from yeast in 2002, which lead to the realization of protein S-acylation being an enzymatic process rather than a simultaneous addition of a long chain fatty acid to proteins, research on S-acylation of proteins has accelerated in a remarkable speed in the past decade
Progress has been made toward understanding various aspects of protein palmitoylation the corresponding research in plants is trailing behind that in yeast and mammals

Summary

Introduction

Lipid modification is a common mechanism in organisms, in which a fatty acid attaches to specific amino acid residues, leading to increased hydrophobicity of proteins which aids their anchoring to membranes or specific lipid rafts (Levental et al, 2010). It seems that cysteine residues in the DHHC-CRD as well as other motifs play joint roles in of PATs auto-acylation and subsequent transfer of the fatty acid to their substrate proteins.

Results

Conclusion