SPalmitoylierung

SPalmitoylation is a post-translational modification involving the addition of a palmitoyl group (a 16-carbon saturated fatty acid) to specific lysine residues within proteins. This modification is crucial for various cellular processes, including protein localization, stability, and function. SPalmitoylation is mediated by enzymes known as palmitoyltransferases, which catalyze the transfer of a palmitoyl group from coenzyme A to the ε-amino group of lysine residues.

The palmitoyl group is attached to the protein through an amide bond, forming an isopeptide linkage. This modification is reversible and can be removed by specific enzymes called palmitoyl-protein thioesterases. SPalmitoylation plays a significant role in the regulation of cell signaling pathways, membrane trafficking, and the organization of the cytoskeleton.

The process of SPalmitoylation is tightly regulated and involves the coordinated action of multiple enzymes and regulatory proteins. Dysregulation of SPalmitoylation has been implicated in various diseases, including cancer, neurodegenerative disorders, and metabolic diseases. Understanding the mechanisms and functions of SPalmitoylation is essential for developing targeted therapies for these conditions.