Palmitoylproteomics

Palmitoylproteomics refers to the study of palmitoylation, a reversible post-translational modification where a palmitate (a 16-carbon fatty acid) is attached to cysteine residues of proteins. This process is mediated by palmitoyl acyltransferases (PATs) and reversed by depalmitoylases (DAPs). Palmitoylation is the most abundant and dynamic lipid modification of proteins in eukaryotes.

The field of palmitoylproteomics aims to identify and quantify palmitoylated proteins within a cell or organism, as well as to understand the specific cysteine residues that are modified. This is typically achieved using mass spectrometry-based techniques. These methods often involve bioorthogonal chemical labeling strategies or affinity purification of palmitoylated proteins followed by proteolytic digestion and mass spectrometric analysis.

The functional consequences of palmitoylation are diverse and include regulating protein trafficking, membrane association, protein-protein interactions, and protein stability. It plays crucial roles in various cellular processes such as signal transduction, synaptic plasticity, and protein sorting. Understanding the palmitoylome, the complete set of palmitoylated proteins in a cell, provides insights into cellular signaling pathways and disease mechanisms. Research in palmitoylproteomics is essential for deciphering the intricate roles of lipidation in cellular function and dysfunction.