Palmitoylating

Palmitoylating is a post-translational modification where a palmitoyl group, a sixteen-carbon saturated fatty acid, is attached to a protein. This process, also known as S-palmitoylation, occurs on cysteine residues within proteins, although other amino acids can be palmitoylated to a lesser extent. The attachment is typically reversible, mediated by a family of enzymes called palmitoyl acyltransferases (PATs) for addition and acyl-protein thioesterases (APTs) for removal.

The addition of the palmitoyl group significantly alters the protein's properties. It increases hydrophobicity, which can promote protein-membrane association or facilitate the formation of protein-protein interactions within lipid bilayers. Palmitoylation plays a crucial role in regulating protein localization, trafficking, stability, and activity. It is involved in a wide array of cellular processes including signal transduction, synaptic plasticity, protein sorting, and viral entry.

The reversibility of palmitoylation allows for dynamic regulation of protein function in response to cellular signals. For example, proteins that are transiently associated with membranes can be recruited or released through cycles of palmitoylation and depalmitoylation. Dysregulation of palmitoylation has been implicated in various diseases, including cancer and neurological disorders, highlighting its importance in maintaining cellular homeostasis.