DHHCpalmitoyltransferaaseiksi

DHHCpalmitoyltransferases, often abbreviated as DHHC enzymes, are a family of integral membrane proteins found in eukaryotic cells. Their primary function is to catalyze the S-palmitoylation of other proteins. Palmitoylation is a post-translational modification where a palmitate molecule, a fatty acid, is covalently attached to a cysteine residue in a target protein. This process is reversible and plays a crucial role in regulating protein localization, trafficking, stability, and interactions.

The DHHC family is characterized by a conserved Asp-His-His-Cys (DHHC) motif within their catalytic domain, which is essential for their enzymatic activity. These enzymes are typically found in the endoplasmic reticulum, Golgi apparatus, and plasma membrane, reflecting the cellular locations where palmitoylation events often occur. They exhibit a broad substrate specificity, meaning a single DHHC enzyme can palmitoylate multiple different proteins, and a single protein can be palmitoylated by several different DHHC enzymes.

The regulation of protein palmitoylation by DHHC enzymes is critical for a wide range of cellular processes, including signal transduction, neuronal function, membrane protein trafficking, and protein sorting. Dysregulation of DHHC enzyme activity has been implicated in various diseases, including cancer, neurological disorders, and infectious diseases, highlighting their importance in cellular homeostasis and disease pathogenesis. Research into DHHC enzymes continues to uncover their diverse roles and potential as therapeutic targets.