ABSTRACT: Protein palmitoylation, also known as S-acylation, is a reversible post-translational modification in which fatty acids are covalently attached to cysteine residues via thioester bonds. To date, protein palmitoylation has been well studied in animal cells, where it plays a crucial role in regulating cell signaling, communication, energy metabolism, innate immunity, neurological diseases, and cancer, among others. Similarly, studies in plants have demonstrated that palmitoylation contributes to the regulation of plant growth and development, adaptation to abiotic stress, and plant immunity. These studies suggest that palmitoylation is an evolutionarily conserved modification with important roles in both animal and plant cells. Although progress has been made in understanding palmitoylation in plants, its investigation has remained relatively limited. Recent study in Arabidospis has shown that more than thounds of proteins undergo palmitoylation in Arabidopsis, highlighting its significant role in plants. However, this number may be an underestimate. According to the SwissPalm database, which catalogs palmitoylated proteins, more than 5,000 mammalian proteins are likely modified by palmitoylation. Additionally, proteome-wide studies in crops have not been investigated, which hinders understanding of its functional roles. To bridge this gap, we selected the monocot model plant Oryza sativa (rice) to conduct a global analysis of protein palmitoylation under basal conditions. Additionally, we quantified the extent of palmitoylation in response to cold stress and explored the novel role of palmitoylation in regulating cytosolic translation.
Qiutao Xu 