Yuhuan Ji, Graduate Student
Mass Spectrometry Resource
Department of Biochemistry
Boston University School of Medicine
670 Albany Street, Suite 504
Boston, MA 02118
S-palmitoylation is a reversible, dynamic lipid modification of proteins. Cycle between palmitoylation and depalmitoylation regulates several important intracellular events such as protein sorting, trafficking, anchoring, stability, and protein-protein interactions. Palmitoylation analyses are often done indirectly, using either the acyl-biotinyl exchange (ABE) method, or metabolic labeling with a palmitic acid analog and the “click” chemistry. Each method has its own advantages and limitations. Additionally, palmitoylation can be easily lost during sample preparation steps, owing to the labile nature of the thioester linkage. Yuhuan’s research focuses on the development of an LC/MS/MS method for direct characterization of protein palmitoylation to minimize false positives or palmitoyl losses during sample preparation steps. Both top-down and bottom-up approaches will be utilized.
Oxidative post-translational modifications (OPTMs) of cysteine residues play a crucial role in redox regulation and signal transduction in both physiological and pathological states. As the thiol group is the primary target for both OPTMs and palmitoylation, it is of great interest to study protein palmitoylation under oxidative stress. In a collaboration with Dr. Cohen and Dr. Bachschmid’s group at the Department of Medicine, Yuhuan is also interested in studying the interplay between OPTMs and palmitoylation, particularly during the development of cardiovascular dysfunctions.