S-palmitoylation is a reversible post-translational modification that adds palmitic acid onto cysteine residues of proteins through the formation of a thioester bond. The reaction is catalyzed by protein acyl transferases (PATs) and reversed by acyl protein thioesterases (APTs), also known as S-depalmitoylases. Here, we optimized acyl resin-assisted capture (acyl-RAC) for identifying S-palmitoylated proteins in the model eukaryote Dictyostelium discoideum. Using this optimized protocol and western blotting, we revealed S-palmitoylated proteins in D. discoideum including calcium-dependent cell adhesion protein A (CadA), calreticulin (CalR), and glucose-regulated protein 78 (Grp78). Overall, this work establishes acyl-RAC as a tool for studying S-palmitoylation in D. discoideum and reveals a subset of S-palmitoylated proteins in this model organism that can be further studied.
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Samer A. Owiar
William David Kim
Robert J. Huber
Biochemistry and Cell Biology
Trent University
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Owiar et al. (Wed,) studied this question.
www.synapsesocial.com/papers/69fd7e90bfa21ec5bbf06de8 — DOI: https://doi.org/10.1139/bcb-2026-0052