Spalmitoilálás

Spalmitoilálás is a post-translational modification that occurs in biological systems. It involves the covalent attachment of a palmitoyl group, a 16-carbon saturated fatty acid, to a protein. This process is catalyzed by enzymes known as palmitoyltransferases, which typically transfer the palmitoyl group from palmitoyl-CoA to cysteine residues within target proteins. However, palmitoylation can also occur on serine and threonine residues, though less commonly.

The addition of a palmitoyl chain significantly alters the physicochemical properties of a protein. It increases its lipophilicity, which can promote its association with cellular membranes. This membrane association is crucial for various cellular functions, including protein trafficking, signal transduction, and protein-protein interactions. Palmitoylation can also influence protein stability, conformation, and localization within the cell.

The removal of the palmitoyl group is carried out by depalmitoylases, also known as acyl-protein thioesterases (APTs). This dynamic process of addition and removal allows for the regulation of protein activity and localization in response to cellular signals. Palmitoylation plays a role in a wide range of biological processes, including neuronal development, immune responses, and viral infection. Aberrant palmitoylation has been implicated in various diseases, making it a subject of ongoing research.